ID A0A3C0D9W1_9BACT Unreviewed; 1112 AA. AC A0A3C0D9W1; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 19-JAN-2022, entry version 12. DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382}; DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382}; GN ORFNames=DCL96_10705 {ECO:0000313|EMBL:HAH92147.1}; OS Prevotella sp. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; unclassified Prevotella. OX NCBI_TaxID=59823 {ECO:0000313|EMBL:HAH92147.1, ECO:0000313|Proteomes:UP000258952}; RN [1] {ECO:0000313|EMBL:HAH92147.1, ECO:0000313|Proteomes:UP000258952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10784 {ECO:0000313|EMBL:HAH92147.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with CC the SecYEG preprotein conducting channel. Has a central role in CC coupling the hydrolysis of ATP to the transfer of proteins into and CC across the cell membrane, serving as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across the CC membrane. {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + CC cellular protein(Side 2).; EC=7.4.2.8; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01382}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF. Other proteins may also be involved. CC {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50. CC {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650, CC ECO:0000256|HAMAP-Rule:MF_01382}. 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:HAH92147.1}. 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; DMGU01000060; HAH92147.1; -; Genomic_DNA. DR Proteomes; UP000258952; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule. DR GO; GO:0017038; P:protein import; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule. DR CDD; cd18803; SF2_C_secA; 1. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01382; SecA; 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004027; SEC_C_motif. DR InterPro; IPR000185; SecA. DR InterPro; IPR020937; SecA_CS. DR InterPro; IPR011115; SecA_DEAD. DR InterPro; IPR014018; SecA_motor_DEAD. DR InterPro; IPR011130; SecA_preprotein_X-link_dom. DR InterPro; IPR044722; SecA_SF2_C. DR InterPro; IPR011116; SecA_Wing/Scaffold. DR InterPro; IPR036266; SecA_Wing/Scaffold_sf. DR InterPro; IPR036670; SecA_X-link_sf. DR PANTHER; PTHR30612; PTHR30612; 1. DR Pfam; PF02810; SEC-C; 1. DR Pfam; PF07517; SecA_DEAD; 1. DR Pfam; PF01043; SecA_PP_bind; 1. DR Pfam; PF07516; SecA_SW; 1. DR PRINTS; PR00906; SECA. DR SMART; SM00490; HELICc; 1. DR SMART; SM00957; SecA_DEAD; 1. DR SMART; SM00958; SecA_PP_bind; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01382}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP- KW Rule:MF_01382}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 4..783 FT /note="SECA_MOTOR_DEAD" FT /evidence="ECO:0000259|PROSITE:PS51196" FT DOMAIN 179..338 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 611..799 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT NP_BIND 195..199 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT REGION 1062..1102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 41..64 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 336..363 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 617..637 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 177 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" FT BINDING 705 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382" SQ SEQUENCE 1112 AA; 127372 MW; 478C5947A7738680 CRC64; MNFNKILQSL FGNKSTRDMK LIQPIVEKIK AEYPKMQALS NDELRAKTKE LQKYVQEYAK EEKAKIAELK AKIEDTPIDE REGIFNQIDK LEQEALDKYE EALNEVLPQV FAIVKDTARR FAENEETIVT ATDFDRELAS NPANDFVTID GDKAIYHNHW TAGGNDMKWE MIHYDVQLFG GVVLHQGKIA EMATGEGKTL VGTTPIFLNA LTGNGVHVVT VNDYLAKRDS EWMGPLYMFH GLSVDCIDKH RPNSDERRKA YLADITFGTN NEFGFDYLRD NMATNPADLV QRQHNYAIVD EVDSVLIDDA RTPLIISGPI PKGDDQMFEQ YQPLVEKLYE VQRKQATELL AEAKQKINEG TKAKNQELLD EGFLALFRSY KALPKNKPLI KYLSEEGIKA GLLKTEEYYM ANNNREMPKA TEPLYFVVDE KMNSADLTDK GTDWLAKQVN DKELFVLPDI TTEMSELEAR TDLTDQERLD KKDEMLAHYG VQSERVHTLQ QLLKGYTMFN KDDEYVVMDG QVKIVDEQTG RIMEGRRWSD GLHQAIEAKE HVKVEAATQT FATITLQNYF RMYHKLAGMT GTASTESGEF WDIYKLDVVE IPTNRPIQRK DLDDRVYKTA REKYRAVIDE IEETRNAGRP VLVGTTSVEI SELLSKMLKM RNIPHNVLNA KLHQQEAQIV AEAGRSVNGK GAVTIATNMA GRGTDIKLTP EVKAAGGLAI IGTERHESRR VDRQLRGRAG RQGDPGSSVF YVSLEDKLMR LFASERIAKV MDRLGFEDGE RIESPMISKS IERAQRKVEE NNFGIRKHLL EYDDVMNRQR TVIYEKRRHA LMGERIGMDI ANIIWDRVLN IVNNNDFFGA KEEFLKVLAM EIPFNEDEYE NGRREDLAER AFQEAMATFK RKTDRIQATA MPIIKQVYEN QGAIYERIMV PITDGKRMYN IPCNLKEAYE SEAKNVVKEF EKSVVLQIID DDWKENLRKL DELKHSVQNA SYEQKDPLLI FKLESAKVWD AMINDMYDRI ASILMRGQIP VMEQEQPVQE AAPEQHTQQN YVESKVDLDA EREAQEAAAN QDTREGAQVN RTPYRAEHMP RPNDPCPCGS GKKFKNCHGR NL //