ID   SECA1_MYCSJ             Reviewed;         947 AA.
AC   A3PWB2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, 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=Mjls_1387;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) 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: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 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}. Note=Distribution is 50-50.
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; CP000580; ABN97189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PWB2; -.
DR   SMR; A3PWB2; -.
DR   STRING; 164757.Mjls_1387; -.
DR   PRIDE; A3PWB2; -.
DR   KEGG; mjl:Mjls_1387; -.
DR   HOGENOM; CLU_005314_3_0_11; -.
DR   OMA; MVHYDVQ; -.
DR   BioCyc; MSP164757:G1G8C-1402-MON; -.
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; -; 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; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Translocase; Translocation; Transport.
FT   CHAIN           1..947
FT                   /note="Protein translocase subunit SecA 1"
FT                   /id="PRO_0000318384"
FT   REGION          860..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         101..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         490
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   947 AA;  106334 MW;  1BDA29A4E6189CA9 CRC64;
     MLDKLLRLGE GRMVKRLKKV ADYVNTLSDD VEKLSDAELR AKTDEFRKRI DGGEDLDDLL
     PEAFAVAREA AWRVLSQRHF DVQVMGGAAL HFGNVAEMKT GEGKTLTCVL PAYLNALSGK
     GVHVVTVNDY LAKRDAEWMG RVHRFLGLDV GVILSGLTPD ERRAAYHADI TYGTNNEFGF
     DYLRDNMAHR LEDRVQRGHN FAVVDEVDSI LIDEARTPLI ISGPADAASN WYSEFARLAP
     LMEKDVHYEV DLRKRTVGVH EVGVEFVEDQ LGIENLYEAA NSPLVSYLNN ALKAKELFQR
     DKDYIVRNGE VLIVDEFTGR VLLGRRYNEG MHQAIEAKEH VEIKAENQTL ATITLQNYFR
     LYDKLAGMTG TAQTEAAELH EIYKLGVVPI PTNRDMIRQD QTDLIYKTEE AKFIAVVDDV
     YERYEKGQPV LIGTTSVERS EYLSKQFTKR KIPHNVLNAK YHEQEANIIA EAGRLGAITV
     ATNMAGRGTD IVLGGNVDFL ADKRLREQGL DPIETPEEYE AAWESTLNQI KAEAEEEADD
     VRAVGGLYVL GTERHESRRI DNQLRGRSGR QGDPGESRFY LSLGDELMRR FNGATLEALL
     TRLNLPDDVP IEAKMVTRAI KSAQTQVEQQ NFEVRKNVLK YDEVMNQQRK VIYEERRRIL
     EGEDLAEQAH KMLVDVVTAY VNGATAEGYA EDWDLEQLWT ALKQLYPVGI DYHDLVDSDA
     VGEAGELTRE ELLDMLIKDA ERAYAERERE LEELAGEGAM RQLERNVLLN VIDRKWREHL
     YEMDYLKEGI GLRAMAQRDP LVEYQREGYD MFVGMLEALK EESVGFLFNV TVEAAPPAPS
     NRVAPVAAPP GLSEFAAAAA KAQEQTGQGA VATKERETPA PTLRAKGIDN DDTPPLTYVG
     PGEDGTAEVQ RSNGGPRHAA PGGATRRERR EAARKQAKTS KPTRRRG