ID A0A3E0TLJ4_9GAMM Unreviewed; 440 AA.
AC A0A3E0TLJ4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN ECO:0000313|EMBL:REL25396.1};
GN ORFNames=DXX92_01625 {ECO:0000313|EMBL:REL34146.1}, DXX93_01750
GN {ECO:0000313|EMBL:REL25396.1}, DXX94_09545
GN {ECO:0000313|EMBL:REL30944.1};
OS Thalassotalea euphylliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL25396.1, ECO:0000313|Proteomes:UP000256478};
RN [1] {ECO:0000313|Proteomes:UP000256478, ECO:0000313|Proteomes:UP000256899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:REL25396.1,
RC ECO:0000313|Proteomes:UP000256478}, H2 {ECO:0000313|EMBL:REL34146.1,
RC ECO:0000313|Proteomes:UP000256999}, and H3
RC {ECO:0000313|Proteomes:UP000256899};
RA Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT "Thalassotalea euphylliae genome.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REL30944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H3 {ECO:0000313|EMBL:REL30944.1};
RA Ferrada E.E., Latorre B.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC proteins may be involved. Interacts with SecA. {ECO:0000256|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|HAMAP-Rule:MF_01465,
CC ECO:0000256|RuleBase:RU004349}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REL25396.1}.
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DR EMBL; QUOU01000001; REL25396.1; -; Genomic_DNA.
DR EMBL; QUOT01000001; REL30944.1; -; Genomic_DNA.
DR EMBL; QUOV01000001; REL34146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0TLJ4; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000256478; Unassembled WGS sequence.
DR Proteomes; UP000256899; Unassembled WGS sequence.
DR Proteomes; UP000256999; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR NCBIfam; TIGR00967; 3a0501s007; 1.
DR PANTHER; PTHR10906:SF9; PREPROTEIN TRANSLOCASE SUBUNIT SCY1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01465};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01465}; Reference proteome {ECO:0000313|Proteomes:UP000256899};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01465}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 396..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 440 AA; 48065 MW; 76A639207637B17E CRC64;
MAKPGTDKAQ GGLTELKQRL WFVVLALIVF RLGSFVPIPG IDAAVLAQLF EQQKGTIVEM
FNMFSGGALE RASVLALGIM PYISASIIMQ LLTVVHPAMA ELKKEGEAGR RKISQYTRYG
TLVLATVQSI AIARGLPAMM PGLVINEGMG FYFTAVVSLV TGTMFLMWLG EQITERGIGN
GISILIFAGI VAGMPSAVGQ TAEMARQGEL HLLVLLLIAV IVFAVTFFVV FVERGQRRIV
VNYAKRQQGR KVFAAQSTHL PLKVNMAGVI PPIFASSIIL FPGTLANWFG QGDGAVADFF
QNLSMAISPG QPLYVMLLAA AIIFFCFFYT ALVFNPRETA DNLKKSGAFI PGIRPGEQTS
KYIDKVMTRL TLAGALYITF ICLVPEFMMI AWDVQFYFGG TSLLIIVVVI MDFMAQVQTH
LMSHQYDSVL KKANLKGYGR
//
