ID   SECA_CYTFI              Reviewed;         473 AA.
AC   P96313;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000250};
DE            EC=7.4.2.8 {ECO:0000250};
DE   Flags: Fragment;
GN   Name=secA {ECO:0000250};
OS   Cytobacillus firmus (Bacillus firmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=1399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bauer M., Baeuerlein E.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=May bind 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer and homodimer (By similarity). Part of the essential
CC       Sec protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Distribution is 50-50. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000305}.
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DR   EMBL; X99401; CAA67777.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96313; -.
DR   SMR; P96313; -.
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-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   CDD; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004027; SEC_C_motif.
DR   InterPro; IPR000185; SecA.
DR   InterPro; IPR020937; SecA_CS.
DR   InterPro; IPR014018; SecA_motor_DEAD.
DR   InterPro; IPR044722; SecA_SF2_C.
DR   InterPro; IPR011116; SecA_Wing/Scaffold.
DR   InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR   PANTHER; PTHR30612; PTHR30612; 1.
DR   Pfam; PF02810; SEC-C; 1.
DR   Pfam; PF07516; SecA_SW; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW   Nucleotide-binding; Protein transport; Translocase; Translocation;
KW   Transport; Zinc.
FT   CHAIN           <1..473
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109575"
FT   REGION          424..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         468
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   473 AA;  54466 MW;  F229F9D0EE1B4234 CRC64;
     KLAGMTGTAK TEEEEFRNIY GMDVMVIPTN KPIARIDKPD LIYKTMEAKF RAVVNEIEEI
     HKKGQPVLVG TVSVETSELV SKLLNKRRVP HHVLNAKNHE REAEIIEGAG QQGAVTIATN
     MAGRGTDIKL GEGVRELGGL HVLGTERHES RRIDNQLRGR AGRQGDPGSS QFYLSMEDEL
     MRRFGSDNMR SMMERLGMEE DQPIESRLVS RAVETAQKRV EGNNFDARKQ ILQYDDVMRE
     QREIIYKQRM EVLESDNLRK IVETMIKDVI DRTVRLHTPE NEVPEDWDLM AIVNYMNANL
     LQEGELEEKD IKGLDPEEMV EAITEKVIAR YNEKEEQFTP EHMREFEKVI MLRTVDRKWM
     NHIDQMDQLR QGIHLRAYGQ NDPLREYRFE GFEMFEAMIA SIEEEVSMYI MKAQVQQNLE
     RQKVAEGKAV HQDTSKQEPK KKQPIRKGET IGRNDACICG SGKKYKNCCG AGK