ID   SECA_PROM3              Reviewed;         951 AA.
AC   A2C5Z6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=P9303_01511;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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:0000255|HAMAP-Rule:MF_01382}.
CC   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC       cells. {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   -!- 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: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       Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {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; CP000554; ABM76906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C5Z6; -.
DR   SMR; A2C5Z6; -.
DR   STRING; 59922.P9303_01511; -.
DR   EnsemblBacteria; ABM76906; ABM76906; P9303_01511.
DR   KEGG; pmf:P9303_01511; -.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   BioCyc; PMAR59922:G1G80-145-MON; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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   Nucleotide-binding; Protein transport; Thylakoid; Translocase;
KW   Translocation; Transport.
FT   CHAIN           1..951
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318407"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         108..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         509
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   951 AA;  107486 MW;  D9640B82E4BD86D0 CRC64;
     MLKLLLGDPN ARKLKRYQPI VTDINILEED IALLSDDQLR SKTADFRQQF ENVVSFPKQR
     VLLDELLPEA FAVVREAAKR VLGMRHFDVQ LIGGMVLHEG QIGEMKTGEG KTLVATLPSY
     LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMSPAERR RNYACDITYA
     TNSELGFDYL RDNMATDLSE VVQREFQYCV IDEVDSILID EARTPLIISG QVERPQEKYQ
     QAADVAAALE RAAEQGKDGI DPEGDYEVDE KQRSCTLTDE GFAKAEQNLK VRDLFDPADP
     WAHYITNALK AKELFVRDVN YIVRDGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEQLAI
     QPETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY KLETSVIPTN QPRARADWVD
     QVYKTESAKW RAVANETAEI HKQGRPVLVG TTSVEKSELL SSLLSEQEIP HNLLNAKPEN
     VEREAEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLP RLVRPEEGHR
     PPVPLQRAAE TGGGFAAKAA ASNGSHGHVL SEARAIGSLY PCSLTDDTDQ FLAELARELV
     KVWGDRALSV IELEDRISTA AEKAPTDDAQ IAALRESIAR VKTEYDVVVT QEEVRVREAG
     GLHVIGTERH ESRRVDNQLR GRAGRQGDLG STRFFLSLED NLLRIFGGER VASLMNAFRV
     EEDMPIESGM LTRSLEGAQK KVETYYYDIR KQVFEYDEVM NNQRRAVYAE RRRVLEGRGL
     KKQVIGYGER TMDDVVEAYV NPDLPPEEWD LDQLVSKVQE FVYLLEDLKP EQLQGLSMEE
     LKSFLQEQLR NAYDIKEGQI EQQRPGLMRE AERFFILQQI DTLWREHLQA MDALRESVGL
     RGYGQKDPLI EYKNEGYDMF LEMMANMRRN VIYSMFMFQP APAPAQEAAN V