ID A0A3C0D9W1_9BACT Unreviewed; 1112 AA. AC A0A3C0D9W1; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 10-APR-2019, entry version 3. DE RecName: Full=Protein translocase subunit SecA {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. OX NCBI_TaxID=59823 {ECO:0000313|EMBL:HAH92147.1}; RN [1] {ECO:0000313|EMBL:HAH92147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA10784 {ECO:0000313|EMBL:HAH92147.1}; RX PubMed=30148503; DOI=10.1038/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 RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. Has a central role CC in coupling the hydrolysis of ATP to the transfer of proteins into CC and across the cell membrane, serving as an ATP-driven molecular CC motor driving the stepwise translocation of polypeptide chains CC across the membrane. {ECO:0000256|HAMAP-Rule:MF_01382, CC ECO:0000256|SAAS:SAAS00093249}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00611882}; 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- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_01382}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382, CC ECO:0000256|SAAS:SAAS00572599}. Note=Distribution is 50-50. CC {ECO:0000256|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|HAMAP- CC Rule:MF_01382, ECO:0000256|SAAS:SAAS00572543}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 CDD; cd00079; HELICc; 1. DR HAMAP; MF_01382; SecA; 1. 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; 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; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463730}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463739}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463758}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463792}; KW Metal-binding {ECO:0000256|SAAS:SAAS00093234}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463805}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463763}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463726}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01382, KW ECO:0000256|SAAS:SAAS00463816}; Zinc {ECO:0000256|SAAS:SAAS00463735}. FT DOMAIN 4 783 SECA_MOTOR_DEAD. {ECO:0000259|PROSITE: FT PS51196}. FT NP_BIND 192 199 ATP. {ECO:0000256|HAMAP-Rule:MF_01382}. FT COILED 41 64 {ECO:0000256|SAM:Coils}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. FT COILED 617 637 {ECO:0000256|SAM:Coils}. 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 //