ID   SECA_AZOC5              Reviewed;         924 AA.
AC   A8IHQ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=AZC_3307;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-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 + H(2)O + cellular protein(Side 1) = ADP + phosphate +
CC         cellular protein(Side 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; AP009384; BAF89305.1; -; Genomic_DNA.
DR   RefSeq; WP_012171830.1; NC_009937.1.
DR   AlphaFoldDB; A8IHQ3; -.
DR   SMR; A8IHQ3; -.
DR   STRING; 438753.AZC_3307; -.
DR   EnsemblBacteria; BAF89305; BAF89305; AZC_3307.
DR   KEGG; azc:AZC_3307; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_5; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000000270; 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..924
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000320730"
FT   NP_BIND         105..109
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   REGION          886..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           908
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           910
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           919
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   METAL           920
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         87
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         517
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   924 AA;  103959 MW;  B728C81A1D3CA342 CRC64;
     MLGGLARKIF GSANDRRVRG YRPSVEAINK LEPELETLTD EQLRERTVMF RQQLAEGKTL
     DDLLVPAFAT VREAAKRVMG MRHFDVQLIG GMVLHDAGIA EMRTGEGKTL VATLPVYLNA
     LAGKGVHVVT VNDYLARRDA EWMAKVYGFL GLTTGIIVHG LDDDQRRAAY ACDVTYATNN
     ELGFDYLRDN MKYERAQMVQ RPHYFAIVDE VDSILIDEAR TPLIISGPLD DRSDFYNTID
     KFIPRLSKGD YEVDEKQRSV AMTEAGMEKM EQMLTEAELL KSGSLYDIEN VSIVHHVNQA
     LRAHSLFQRD KDYIVRNDEV VIIDEFTGRM MPGRRYSEGL HQALEAKERV TVQPENQTLA
     SITFQNYFRL YERLGGMTGT AATEAAEFAD IYKLDVVEIP TNRKVQRIDD DDEVYRTNRE
     KFDAIVKLIQ ECAARKQPVL VGTTSIEKSE LLAERLKQAG MRQKDFSDRA AFTGSSDGKS
     FAVLNARYHE QEAFIVAQAG VPGAVTIATN MAGRGTDIQL GGNAEMRISE ELADLPAGPE
     REAAEAKIRE EIAALKQEAL AAGGLFVLGT ERHESRRIDN QLRGRSGRQG DPGHSKFFLS
     LEDDLMRIFG SDRLEGMLKR LGLQEGEAII HPWINRALEK AQQKVEARNY DMRKNVLKYD
     DVLNDQRKVV FEQRLELMND EDVAETVVDM RHDVITDLVA KYIPVNSYPE QWDVKGLDFA
     VRDVLTLALP IEDWAKEEGI AGPEVTERII QKADEWMASK SAQYGPELMR YVEKSILLQT
     LDHLWREHIA MLDHLRQVIG LRGYGQRDPL QEYKSEAFQL FSAMLGRLRE IVTAQLMRVE
     IVSTPQPTEL PPMEAHHIDA STGEDELASA GAALSARPEL ALATEVPAAD RDPNDPSTWG
     KVGRNEPCPC GSGKKFKHCH GRFA
//