ID Q9CL50_PASMU Unreviewed; 441 AA. AC Q9CL50; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 04-NOV-2026, entry version 131. DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|ARBA:ARBA00039733, ECO:0000256|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465, GN ECO:0000313|EMBL:AAK03479.1}; GN OrderedLocusNames=PM1395 {ECO:0000313|EMBL:AAK03479.1}; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK03479.1, ECO:0000313|Proteomes:UP000000809}; RN [1] {ECO:0000313|EMBL:AAK03479.1, ECO:0000313|Proteomes:UP000000809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK03479.1, RC ECO:0000313|Proteomes:UP000000809}; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). 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 inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01465}. Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU003484}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004439; AAK03479.1; -; Genomic_DNA. DR RefSeq; WP_010907153.1; NC_002663.1. DR STRING; 272843.PM1395; -. DR EnsemblBacteria; AAK03479; AAK03479; PM1395. DR KEGG; pmu:PM1395; -. DR PATRIC; fig|272843.6.peg.1407; -. DR HOGENOM; CLU_030313_0_2_6; -. DR OMA; AAGNQSM; -. DR OrthoDB; 9809248at2; -. DR FunFam; 1.10.3370.10:FF:000001; Preprotein translocase subunit SecY; 1. 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 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 NCBIfam; TIGR00967; 3a0501s007; 1. DR PROSITE; PS00755; SECY_1; 1. DR PROSITE; PS00756; SECY_2; 1. 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 Proteomes; UP000000809; Chromosome. DR AlphaFoldDB; Q9CL50; -. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01465}; 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:UP000000809}; 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 21..39 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 75..98 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 119..140 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 184..201 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 213..235 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 272..293 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 313..333 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 371..389 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 395..416 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" SQ SEQUENCE 441 AA; 48147 MW; B0891439C022C0CA CRC64; MAKQPGYQSR STQSGTGELK SRLLFVLGAL IVFRIGSFIP VPGIDAAVLA QLVEQQKGTI IDMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTTVHP ALAELKKEGE AGRRKISKYT RYSTLVLATL QAVGISTGLP NMLPGLVPNV GFSFYLAAVI SLVTGTMFLM WLGEQITERG IGNGISLIIF AGIVAGLPSA IGQTIEQTRQ GQMHLLVLLL IAVIVFAVTY FVVFVERGQR RIKVEYAKRQ QGRQILGGHS THLPLKVNMA GVIPAIFASS IILFPATLAQ WLGEGSSLEW LTDLSMLLHP GQPLYLLVYA VAIIFFSFFY TAMQYNPRDT ADNLKKSGAF IPGIRPGEQT SRYIDKIMTR LTLIGGLYIT FVCLVPYVMT SAWNVQFYFG GTSLLIVVVV IMDFIAQVQS HLMSTKYESA LKKANLKGFG Q //