ID   SECA_PROM1              Reviewed;         944 AA.
AC   A2C591;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=NATL1_20951;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
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; CP000553; ABM76651.1; -; Genomic_DNA.
DR   RefSeq; WP_011824595.1; NC_008819.1.
DR   AlphaFoldDB; A2C591; -.
DR   SMR; A2C591; -.
DR   STRING; 167555.NATL1_20951; -.
DR   PRIDE; A2C591; -.
DR   EnsemblBacteria; ABM76651; ABM76651; NATL1_20951.
DR   KEGG; pme:NATL1_20951; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   Proteomes; UP000002592; 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..944
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318411"
FT   REGION          533..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   944 AA;  107930 MW;  E0A57C52874A6F78 CRC64;
     MFKKLLGDPN TRKLKRYFPL VSDVNIFEED LLSLSDDDLR TRTSEFRSKL EKVSSPNEEL
     SLLDELLPEA FAVVREASKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPSY
     LNALTGRGVH VVTVNDYLAR RDAEWMGQIH RFLGLSVGLV QQSMAPLERK KNYECDITYA
     TNSELGFDYL RDNMAADKSE IVQRDFQFCV IDEVDSILID EARTPLIISG QVERSQEKYK
     QAAQVVENLK RAIDTSKDGI DPEGDYEVDE KQRSCILTDE GFANTEKLLN VQDLFDPKEP
     WAHYVTNALK AKELFIKDVN YIVRNDEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKENLSI
     QPETQTLASI TYQNFFLLYP RLSGMTGTAK TEEVEFEKTY KLQTTVVPTN RKISRQDWVD
     QVFKTEAAKW RAVAKETADI HQKGRPVLVG TTSVEKSELL STLLSEQQVP HNLLNAKPEN
     VEREAEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKIKEILSN RLVKPEEGHK
     PPVSPQRKTK SAGFKEEKNK NLSISKQNQS KSFLNIFPVS LTEDTDAKLA SLASKLVKEW
     GDRSLSSIEL DDYIATAAEK TPTQDKNIKE LRIAIQLIKN EYEEVLSQEE TNVRRVGGLH
     VIGTERHESR RVDNQLRGRA GRQGDLGSTR FFLSLEDNLL RIFGGDRVAG LMNAFRVEED
     MPIESGMLTR SLEGAQKKVE TYYYDIRKQI FEYDEVMNNQ RKAVYSERRR VLDGRELKLQ
     VIGYGQRTME EIVEAYVNED LPPEEWNLTN LVSKVKEFIY LLEDLKPEDL LGLNKNELKD
     FLKEQLRNAY DMKEAKVEQS HPGIMRQAER FFILQQLDTL WREHLQSMDS LKESVGLRGY
     GQKDPLIEYK NEGYDMFLEM MVNMRRNVIY SMFMFQPAQK KVEA