ID   SECA_SALRD              Reviewed;        1160 AA.
AC   Q2S4E4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SRU_0801;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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   -!- 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       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; CP000159; ABC45488.1; -; Genomic_DNA.
DR   RefSeq; WP_011403566.1; NC_007677.1.
DR   RefSeq; YP_444937.1; NC_007677.1.
DR   AlphaFoldDB; Q2S4E4; -.
DR   SMR; Q2S4E4; -.
DR   STRING; 309807.SRU_0801; -.
DR   EnsemblBacteria; ABC45488; ABC45488; SRU_0801.
DR   KEGG; sru:SRU_0801; -.
DR   PATRIC; fig|309807.25.peg.824; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_0_0_10; -.
DR   OMA; MVHYDVQ; -.
DR   Proteomes; UP000008674; 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: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; -; 3.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000185; SecA.
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   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; Translocase;
KW   Translocation; Transport.
FT   CHAIN           1..1160
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000320983"
FT   REGION          342..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         180..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         726
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1160 AA;  133549 MW;  FE2D18A7A9974553 CRC64;
     MFEWIKNLFG DPNERELNKL WPIVEEINDH YEELQDLTDD ELRAKTDAFR AEIREAVADI
     EARQNEIREK LKRAPGLEGP VGGDGQVTEM EGEALSLDER DALYDEFDEL EEEWQDVVED
     TLWELLPEAF AVVKETCRRM LGETWMAGGS KIEWDMVPYD VQILGAIVLH QGRIAEMKTG
     EGKTLAAVMP LYLNALTGRG CQLVTVNDYL AERDTEWMGP IYEFHGLTVD CVNRYDPHTE
     GRKEAYEADI TYGTNNEIGF DYLRDNSFVV RPEQLMQRGH HYAIIDEIDS VLIDEARTPL
     IISGPVPDQE NDEYRELRDP VEQLVEAQRR LVRSFVKETR ELLEEKEEAE EEGDSRRAQE
     LEDEAGLSLF RASRGYPKNR QLQKLLNEPG MERLRQKTEN FYLQENAKRM PFVDQELYFS
     VDEKKQTVEM TEKGQEYIAK IMDESEDLFV LPVVGDKIAE VEDEYQEKVD ELEEALQEED
     LSQEKRENKY MNDKRELEKE LQETKREIYN TYSERAERVH AIEQLLKAFT LYERDTEYIV
     QEGKVQIVDE HTGRVMEGRR YSEGLHEALE AKEEVEIQNA TQTYASVTLQ NYFRMYDKLS
     GMTGTAETEA EEFNEIYDLD VVVVPTHEPV RRDDKDDLVF QTKREKYNAI VEKVKEYNKR
     GQPVLVGSAS VEVSETISRT LEREGIPHNV LNAKQDRAKE EAQIVAEAGQ KGSVTIATNM
     AGRGTDIQIT DEVRELGGLA ILGSERHESR RIDLQLRGRA GRQGDPGESQ FYVSLEDDLM
     RLFGSDRVAK VMDSMGIEEG EVITHPWINK SIKRAQSKVE QNNFAIRKRQ LEYDDVLNSQ
     REVIYKRRRE ALTGERFHGQ VLNMLYEYIE ALVERHYGQG NIAGLREDLL RTLAFDLEMD
     REEFVQLGED GVVDHVYDVA TDYYRQKRAN IAQPFHQTLR DLKQERGDDM IEQVFVDFTD
     GQDAIRAVAD VDEALETNGE EINEALERTA MLQTIDEKWT DHLRELDELK EGIGLRSFGR
     KDPVVEYKME AFDLFSDMMA EIGQEVVSLV FRAGPVVDDE VQTEGQGPRR RLSQRNAQTQ
     HDSAQPDYSI DADGDGGGGQ EGEAAERDPT VEEKQPVTVA DEPGRNEYVT VRNNANGETT
     EMKWKYAKKK INQGGWSLVS