ID   SECA1_MAGMM             Reviewed;         901 AA.
AC   A0LCX0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Mmc1_3327;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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 both as a receptor for the
CC       preprotein-SecB complex and as an ATP-driven molecular motor driving
CC       the stepwise translocation of polypeptide chains across the membrane.
CC       {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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {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-YajC and YidC. {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; CP000471; ABK45813.1; -; Genomic_DNA.
DR   RefSeq; WP_011714872.1; NC_008576.1.
DR   AlphaFoldDB; A0LCX0; -.
DR   SMR; A0LCX0; -.
DR   STRING; 156889.Mmc1_3327; -.
DR   PRIDE; A0LCX0; -.
DR   EnsemblBacteria; ABK45813; ABK45813; Mmc1_3327.
DR   KEGG; mgm:Mmc1_3327; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_5; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000002586; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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; PF02810; SEC-C; 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   Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocase; Translocation; Transport; Zinc.
FT   CHAIN           1..901
FT                   /note="Protein translocase subunit SecA 1"
FT                   /id="PRO_0000318372"
FT   REGION          847..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         105..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   901 AA;  102548 MW;  CE02311CBC3C794D CRC64;
     MFSAIARKLF GSRNDRYLRS LQPLVDRING LEAEYEALSD SELTAMTYAF KARLEKGETL
     DDLLPEAFAV VREGSKRVLG MRHYDVQLIG GIVLHQGKIS EMKTGEGKTL VATLSLYLNA
     LSGKGAHLVT VNDYLARRDA EWMGKLYQFL GLSVGVIIHG IEDQQRKAAY NADITYGTNN
     EFGFDYLRDN MKFSLEEMVQ RPLNYAIVDE VDSILVDEAR TPLIISGPTE DSTDKYYKVD
     RLIPQLEKER HYTLDEKQRS VTFTEEGNEQ IEQLMRQAGL LRDGDLYDLH NIEMVHHVNQ
     ALKAHAMFEV DRDYIVKDGQ VVIIDEFTGR MMPGRRYSDG LHQALEAKEQ VVIQNESQTL
     ASITFQNLFR LYNKLAGMTG TADTEAAEFQ SIYNLEVVII PTNRDMVRID RDDMVFRTLE
     EKLKAVAEDI KVSYEKGQPV LVGTVSIEKS EMVSHFLKKL KIPHEILNAK HHEREAEIVA
     QAGRPRAVTI ATNMAGRGTD IQLGGNLEMR LKKEIDPEAS PAERTQQEIQ IRTEYEQDKA
     LVLASGGLHI IGTERHESRR IDNQLRGRAG RQGDPGSSGF YLSLQDDLMR IFGSERMDGM
     LKKLGLQDGE AIVHPWINKA VESAQKKVEG RNFDIRKNLL KFDDVMNEQR KVIYDQRKEL
     MENEDIRDFI DEIREEVVHA LVDSHLGEDV YPEEWDAKGF REAMLNQFNL DLNVESWKHE
     EGVTHLVAKE RAMAAVKAYS EAREARLGPP LMRYLEKSIM LQVLDTLWKE HLLNMDHLKE
     GIHLRGYAQK DPLNEYKREA FQLFSMLLQR IREEAIEFLG KVEVQQPEEV AAYEAELAEA
     RNQQMSLNHP ESGSWGGEGE GPSSEGAPHL PFKRDGEKVG RNQACPCGSG KKYKQCCGKL
     S