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There are several matches for 'secretion protein SecY'.
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79 matches
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organism
protein
1)
Escherichia coli K12
secE - Preprotein translocase membrane subunit; Essential subunit of the
protein
translocation channel SecYEG. Clamps together the 2 halves of
SecY
. May contact the channel plug during translocation. Overexpression of some hybrid
proteins
has been thought to jam the
protein
secretion
apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of
SecY
; Belongs to the SecE/SEC61-gamma family.
[a.k.a. b3981, AAC76955.1, Q2M8R7]
2)
Escherichia coli K12
secG - Preprotein translocase membrane subunit; Subunit of the
protein
translocation channel SecYEG. Overexpression of some hybrid
proteins
has been thought to jam the
protein
secretion
apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of
SecY
. Treatment with antibiotics that block translation elongation such as chloramphenicol also leads to degradation of
SecY
and SecE but not SecG.
[a.k.a. AAC76207.1, b3175, Sec translocon subunit SecG]
3)
Ensifer adhaerens
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. OV14_2432, AHK44116.1, AHK44116,
Secretion protein SecY
,
secretion protein SecY
, ...]
4)
Parvularcula bermudensis
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. PB2503_09544, ADM09961.1, ADM09961,
Secretion protein SecY
,
secretion protein SecY
, ...]
5)
Pseudomonas aeruginosa
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. PA4243, AAG07631.1, NZ_QZGE01000028.1,
Secretion protein SecY
,
secretion protein SecY
, ...]
6)
Pseudomonas entomophila
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. PSEEN0510, CAK13456.1, pen:PSEEN0510,
Secretion protein SecY
,
secretion protein SecY
, ...]
7)
Rhodopseudomonas palustris CGA009
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. RPA3230, CAE28671.1, Q6N4V3_RHOPA,
Secretion protein SecY
,
secretion protein SecY
, ...]
8)
Sinorhizobium fredii NGR234
secY -
Secretion
protein
SecY
; The central subunit of the
protein
translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic
SecY
resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore
[a.k.a. NGR_c12100, ACP24992.1, C3MAZ9,
Secretion protein SecY
,
secretion protein SecY
, ...]
9)
Cedecea neteri
syd_2 -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. LH23_01210, AIR59318.1, Secretion protein]
10)
Chania multitudinisentens
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. Z042_06060, AHG19230.1, Secretion protein]
11)
Cronobacter condimenti
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. AFK62_15800, ALB63869.1, Secretion protein]
12)
Cronobacter dublinensis LMG23823
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. ALB67991.1, AFK67_16560, Secretion protein]
13)
Dickeya solani
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. LH89_07325, AIR69033.1, Secretion protein]
14)
Edwardsiella tarda
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. AAW15_12450, AKH89885.1, Secretion protein]
15)
Enterovibrio coralii
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. ATN88_21740, KXF81018.1, Secretion protein]
16)
Erwinia iniecta
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. NG42_13445, KOC89114.1, Secretion protein]
17)
Erwinia mallotivora
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. BG55_14795, EXU74973.1, Secretion protein]
18)
Erwinia sp. Leaf53
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. ASF13_02270, KQN64718.1, Secretion protein]
19)
Erwinia tracheiphila
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. SY86_08100, KKF37778.1, Secretion protein]
20)
Erwinia typographi
syd -
Secretion
protein
; Interacts with the
SecY
protein
in vivo. May bind preferentially to an uncomplexed state of
SecY
, thus functioning either as a chelating agent for excess
SecY
in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family.
[a.k.a. NG99_11465, KGT93283.1, Secretion protein]
79 matches
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