ID SECA_COXBU Reviewed; 913 AA. AC Q83F06; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=CBU_0147; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). 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 both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor driving CC the stepwise translocation of polypeptide chains across the membrane. CC {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01382}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01382}; CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01382}; CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50- CC 50. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP- CC Rule:MF_01382}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO89711.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AE016828; AAO89711.2; ALT_INIT; Genomic_DNA. DR RefSeq; NP_819197.2; NC_002971.3. DR RefSeq; WP_010957404.1; NC_002971.4. DR AlphaFoldDB; Q83F06; -. DR SMR; Q83F06; -. DR STRING; 227377.CBU_0147; -. DR EnsemblBacteria; AAO89711; AAO89711; CBU_0147. DR GeneID; 1208018; -. DR KEGG; cbu:CBU_0147; -. DR PATRIC; fig|227377.7.peg.149; -. DR eggNOG; COG0653; Bacteria. DR HOGENOM; CLU_005314_3_0_6; -. DR OrthoDB; 9805579at2; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC. 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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central. DR CDD; cd17928; DEXDc_SecA; 1. DR CDD; cd18803; SF2_C_secA; 1. DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1. 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 NCBIfam; TIGR00963; secA; 1. DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1. DR Pfam; PF21090; P-loop_SecA; 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; SM00957; SecA_DEAD; 1. DR SMART; SM00958; SecA_PP_bind; 1. DR SUPFAM; SSF81886; Helical scaffold and wing domains of SecA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane; KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome; KW Translocase; Translocation; Transport; Zinc. FT CHAIN 1..913 FT /note="Protein translocase subunit SecA" FT /id="PRO_0000320787" FT REGION 568..588 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 871..913 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 105..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 517 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 897 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 899 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 908 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 909 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" SQ SEQUENCE 913 AA; 103879 MW; E98BDF59F6CFC2D7 CRC64; MLGNIIKKAF GTRNERLLKG YSKIVSRINA LEPEIQALSD ADLRAKTDEF KKRLVDGEGL DALLPEAFAV VRETSVRTLG LRHFDVQIIG GLALHGGKIA EMRTGEGKTL GATMPAYLNA LTGKGVHIVT VNDYLAKRDA EWMKPIYEFL GLTVGVNVPG MEPVEKQAAY AADITYGTNN EFGFDYLRDN MVFDLDQRVQ RPLHYAIIDE VDSILIDEAR TPLIISGQAE ESSDLYVKIN KFIPQLKLQK MEEGQKEEEV PPENRGDYTL DEKNRQAYLT EQGHRTIEAL MIKQGLMQAG ESLYDVSNIS LMHYVYAALR AHTLFYRDVH YIVKNNEVII VDEHTGRLMP GRRWSDGLHQ AVEAKEGATI QLENQTLATI TFQNYFRLYE KLSGMTATAD TEAFELQKIY GLEVVVIPTN RPMIRRDESD QVYLTADAKF DAIVNEVKKR HEKGQPLLIG TASIEASELV ARFLKKANIK HEILNAKNHE REAKIIAEAG RPGAVTIATN MAGRGTDIVL GGNLEAEMSE LDNLAEEEIQ KRKADWQKRH DAVIAAGGLH VLGTERHESR RIDNQLRGRS GRQGDPGSSQ FYLSMEDNLL RIFAAERMSN MMRRLGVKED DVIEHPWITR AIEKAQRRVE GMNFDIRKQL LEYDDVANDQ RKVIYQQRFQ LLQTDDISET IEAIREEAVS EMISSFVPPQ SLEEEWDIPG LEKQIREDFG LALPIAQWLE KDETLHEETL HKRIIDEITK AYKAKEAKAD PKAMREVEKT LMLQLLDHHW KEHLAAMDHL RQGIHLRGYA QKNPAQEYKR ESFELFTQML KRIKYELAAT LSKLEIATEE QVAQQQRLYQ QSAPELQYHH AEMTALQPEK EVAVAEQEEA TQPFVRSQPK VGRNESCPCG SGKKYKQCHG KLS //