ID   SECA_PROM4              Reviewed;         945 AA.
AC   A9BD85;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=P9211_17671;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
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; CP000878; ABX09698.1; -; Genomic_DNA.
DR   RefSeq; WP_012196318.1; NC_009976.1.
DR   AlphaFoldDB; A9BD85; -.
DR   SMR; A9BD85; -.
DR   STRING; 93059.P9211_17671; -.
DR   EnsemblBacteria; ABX09698; ABX09698; P9211_17671.
DR   KEGG; pmj:P9211_17671; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   Proteomes; UP000000788; 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..945
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000145044"
FT   REGION          533..568
FT                   /note="Disordered"
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   945 AA;  107344 MW;  C486A078722AE2D0 CRC64;
     MLKLLLGDPN ARKLKRYLPI VSDINLLEEE ISPLTDDELR AKTADFRERL AKVSGLEKQR
     ELLDEILPEV FSVVREASKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPSF
     LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMTPLERR KNYECDITYA
     TNSELGFDYL RDNMASDMSE IVQRKFQFCI IDEVDSILID EARTPLIISG QIERPQEKYQ
     KAAEVVASLI RAAEMGKDGI DPEGDYEVDE KQRTCTLTDE GFARSEELLK VNDLYDPKDP
     WAHYITNALK AKELFVKDVN YIVRNGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEKLNI
     QSETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY QLETTVIPTN RPRSRNDWVD
     QVYKTEAGKW RAVANETAEV HKKGRPVLVG TTSVEKSELL SSLLAEEQIP HNLLNAKPEN
     VEREAEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLP KLVKPEDGHK
     PPVPLQRRSE SSGFGEDKDV TTDNSKPLSA SSALGTLYPC VLTEDTEKVL IDLERKLVAD
     WGDRALTAIE LEDRISTAAE KAPTNDASIQ LMRDAISLVK SEYDVVVQKE EVQVREAGGL
     HVIGTERHES RRVDNQLRGR AGRQGDLGST RFFLSLGDNL LRIFGGDRVA SLMNAFKVDE
     DMPIESGMLT RSLESAQKKV ETYYYDIRKQ VFEYDEVMNN QRRAVYSERR RVLDGFGLKK
     QVIGYGEKTM EEIVYAYVNP DLPSEEWDLA QLVSKVKEFV YLLNDLKPDQ LEGLDIDELK
     AFLQEQLRNA YDLKEAQIEE QKPGLMKEAE RFFILQQIDT LWREHLQAMD ALRESVGLRG
     YGQKDPLIEY KNEGYDMFLE MMTNMRRNVI YSMFMFQPAP ESDKE