ID   SECA_PROMT              Reviewed;         942 AA.
AC   Q46IG8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=PMN2A_1220;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
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; CP000095; AAZ58710.1; -; Genomic_DNA.
DR   RefSeq; WP_011295564.1; NC_007335.2.
DR   AlphaFoldDB; Q46IG8; -.
DR   SMR; Q46IG8; -.
DR   STRING; 59920.PMN2A_1220; -.
DR   EnsemblBacteria; AAZ58710; AAZ58710; PMN2A_1220.
DR   KEGG; pmn:PMN2A_1220; -.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   PhylomeDB; Q46IG8; -.
DR   Proteomes; UP000002535; 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; Reference proteome; Thylakoid;
KW   Translocase; Translocation; Transport.
FT   CHAIN           1..942
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318412"
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   942 AA;  107409 MW;  207018BCDFEFD626 CRC64;
     MFGQLLGDPN KRRLKNYYPI VSEINILEED ISVLSDEELR GSTNEFRQRL EKAENSDKQL
     KILDELLPNA FAVVREASKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVSTLPSY
     LNALTGKGVH VVTVNDYLAK RDAEWMGQVH RFLGLEVGLI QQDMNPRERK KNYQCDITYA
     TNSELGFDYL RDNMAADKAE IVQRDFQFCV IDEVDSILID EARTPLIISG QVERPQEKYQ
     KAAEVVMKLQ RASELGKDGI DPEGDYEVDE KQRSCVLTDD GFAKTEELLE VKDLFDPKDP
     WAHYVTNALK AKELFTKDVN YIVRNGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKENLAI
     QPETQTLASI TYQNFFLLYP RLSGMTGTAK TEEVEFDKTY KLKTSVIPTN KKVSREDWVD
     QVFKTENAKW RAVAKETSLI NKQGRPILVG TTSVEKSELL STLLAEENIP HNLLNAKPEN
     VERESEIVAQ AGRKGAVTIA TNMAGRGTDI ILGGNSEYMA KLKIKQVLSS RLVKPEDRHN
     PPVPLQRDKA SGFKSLEVKA EAKTSNQSSS LNNLFPVILS DKTDNELGQL AAKLVKEWGD
     RALTLGELED YIATAAEKTP TKDENILAIR RAIHSIKTEY EVITNNEEKL VTEAGGLHVI
     GTERHESRRV DNQLRGRAGR QGDFGSTRFF LSLEDNLLRI FGGDRVAGLM NAFRVEEDMP
     IESGMLTRSL EGAQKKVETY YYDIRKQVFE YDEVMNNQRK AVYSERRRVL KGQELKSQVI
     SYGEKTMGEI VDAYINEELP PEEWELDKLV GKVQEFIYLL NDLKSSELIG LDTNQLKVFL
     QEQMRNAYDL KEAQLEETHP GIMREAEKFF MLQQLDTLWR EHLQSMDSLR ESVGLRGYGQ
     KDPLIEYKNE GYDMFLEMMI NFRRNVIYSM FMFQPTTKKV ES