ID D6YRY8_WADCW Unreviewed; 456 AA. AC D6YRY8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 67. 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:ADI38833.1}; GN OrderedLocusNames=wcw_1484 {ECO:0000313|EMBL:ADI38833.1}; OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044). OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38833.1, ECO:0000313|Proteomes:UP000001505}; RN [1] {ECO:0000313|EMBL:ADI38833.1, ECO:0000313|Proteomes:UP000001505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505}; RX PubMed=20531937; DOI=10.1371/journal.pone.0010890; RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.; RT "The Waddlia genome: a window into chlamydial biology."; RL PLoS ONE 5:E10890-E10890(2010). 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; CP001928; ADI38833.1; -; Genomic_DNA. DR RefSeq; WP_013182541.1; NZ_LVEB01000002.1. DR AlphaFoldDB; D6YRY8; -. DR STRING; 716544.wcw_1484; -. DR KEGG; wch:wcw_1484; -. DR eggNOG; COG0201; Bacteria. DR HOGENOM; CLU_030313_0_0_0; -. DR OrthoDB; 9809248at2; -. DR Proteomes; UP000001505; Chromosome. 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 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:UP000001505}; 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..39 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 75..97 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 118..139 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 159..183 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 195..217 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 229..252 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 285..308 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 328..348 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 384..406 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 412..432 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" SQ SEQUENCE 456 AA; 50748 MW; 85C3FF5BEC463541 CRC64; MIQALQRVFS IPELRQKISF TLLMLVVCRI GAFIPVPGIN GEVAIQYLRH LTGGEQNLFR MVDTFTGGAF SQMTVIALGV VPYISASIMM QLFTALIPSL QREIQENPTL GRRKVNRLTR LVTLILAFIQ SAMFAKYAIQ MNITKPGIIA GDLLNIQMFG HPVLFYAVMI FTMTTGTLFL MWIGEQITEN GIGNGMSLII TLGIISSFPT AIGMIFQQLN LDSQEAGQLN FAIVAVIMAV FVLVTIGTIL IVQGHRRIPL QYARRVVGRK EVQGGNSYIP LKVNYAGVIP VIFASSLLMF PATIATFIGQ GTWLESVAMW FRQDRTAYMV MYVGLIIFFT YFWTATQFRP DQIASDMKKN GAFIPGIRQG RPTQEYLEHT MNRITLIGAV FLALIAILPT ITGRVLGVSQ TISYFFGGTA LLILVGVVLD TMKQIESHLL MKRYEGFMKK GRARGR //