ID   SECA_XANP2              Reviewed;         931 AA.
AC   A7ICM7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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}; OrderedLocusNames=Xaut_0512;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000781; ABS65770.1; -; Genomic_DNA.
DR   RefSeq; WP_012112540.1; NC_009720.1.
DR   AlphaFoldDB; A7ICM7; -.
DR   SMR; A7ICM7; -.
DR   STRING; 78245.Xaut_0512; -.
DR   PRIDE; A7ICM7; -.
DR   EnsemblBacteria; ABS65770; ABS65770; Xaut_0512.
DR   KEGG; xau:Xaut_0512; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_5; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   PhylomeDB; A7ICM7; -.
DR   Proteomes; UP000002417; Chromosome.
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: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   CDD; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
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; 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   TIGRFAMs; TIGR00963; 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..931
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000145078"
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         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         915
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         917
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         926
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         927
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   931 AA;  104677 MW;  8FEE28D424484137 CRC64;
     MLGGLARKLF GSANDRRVKG YRPRVQAINA LEPELEALSD EALRARTEDF RRQLAEGKTL
     DDLLVPAFAT VREGAKRALG MRPFDVQLIG GMVMHEAGIA EMKTGEGKTL VATLPVYLNA
     LAGKGVHVVT VNDYLAKRDA EWMGRLYRFL GLTTGIIVHG LDDDERRVAY ASDVTYATNN
     ELGFDYLRDN MKYERGQMVQ RPHFYAIVDE VDSILIDEAR TPLIISGPLD DRSDFYNTID
     TYIPRLGKED YEVDEKQRSV SMTEAGMEKM EQMLSAAGVL KSASLYDIEN VSVVHHVNQA
     LRAHTLFQRD KDYIVRNDEV VIIDEFTGRM MPGRRYSEGL HQALEAKERV QVQPENQTLA
     SITFQNYFRL YEKLSGMTGT ANTEAAEFAD IYKLEVVEIP TNVQISRIDD DDEVYRTAGE
     KYAAIIELIK ECAERSQPVL VGTTSIEKSE LLAELLKQAG FRQKDFSDPT AFNGRELLIN
     DRSGKSFAVL NARYHEQEAY IVSQAGVPGA ITIATNMAGR GTDIKLGGSA DMRIEIELKD
     LPEGAERAAA EAKIRAEVEE LKQKALEAGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGH
     SKFFLSLDDD LMRIFGSDRL DGMLQRLGLK EGEAIIHPWI NKALEKAQQK VEARNYDMRK
     NVLKYDDVLN DQRKVVFEQR VELMNDEDVA ETVEDMRHAL ITETVAKFIP ENAYPEQWDV
     DGLDTALKEM LALDLPVKDW AKEEGIAGPE VTERIIRRAD ELMAAKTAQY GPDIMRYVEK
     SILLQTLDHL WREHIGMLDH LRQVVGLRGY AQRDPLNEYK SEAFNLFSAL LNRLREVVTA
     QLMRVEIVTQ QPPPEELPPM EAHHADPFTG EDELAFAGAA LGSRPQPLLS GDLAVAERDP
     NDPESWGKVG RNEACPCGSG KKYKHCHGRF A