ID   SECA_CLAM3              Reviewed;         941 AA.
AC   A5CPU4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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=CMM_1054;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01093.1; -; Genomic_DNA.
DR   RefSeq; WP_012037740.1; NC_009480.1.
DR   AlphaFoldDB; A5CPU4; -.
DR   SMR; A5CPU4; -.
DR   STRING; 443906.CMM_1054; -.
DR   EnsemblBacteria; CAN01093; CAN01093; CMM_1054.
DR   GeneID; 56885359; -.
DR   KEGG; cmi:CMM_1054; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_11; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000001564; 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; -; 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..941
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318334"
FT   REGION          880..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         104..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   941 AA;  104567 MW;  6860F7AACA89C0ED CRC64;
     MASVLEKVLR VGEGRTLRKL QNYAKAVNQL EEDFTHLTDE ELKNETVELR ERHANGESLD
     DLLPEAFAAV REASRRTLGL RHFDVQIMGG AALHLGNIAE MKTGEGKTLV ATLPAYLNAI
     ASRGVHVITV NDYLASYQSE LMGRVFRALG MTTGVILAGQ TPQQRREQYA ADITYGTNNE
     FGFDYLRDNM AWQASDMVQR GHFFAVVDEV DSILIDEART PLIISGPSAG DANRWFTEFA
     TVAKRLVPEV DYEVDEKKRT VGVLEAGIEK VEDHLGIDNL YESANTPLIS FLNNSIKAKA
     LFKKDKDYVV MNGEVLIVDE HTGRILMGRR YNEGIHQAIE AKEGVAVKAE NQTLATVTLQ
     NYFRLYKKLS GMTGTAETEA AEFMSTYKLG VVPIPTNRPM QRKDQSDLIY KNEKAKFEQV
     VEDIAERHAA GQPVLVGTTS VEKSEYLSKL LAKKGVRHEV LNAKNHAREA AIVAQAGRLG
     SVTVATNMAG RGTDIMLGGN AEFLAVAAMN ARGLSPVETP EQYETEWDDV FADVKAEVDE
     EAAKVIEAGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLTDD LMRLFNNGAA
     ASLMGRDSVP DDVAIESKVV SRAIRSAQGQ VEARNAEIRK NVLKYDDVLN RQREAIYGDR
     RHILEGDDLQ ERSQRFLEAV IDDVLDSHIG EGNGDDWDFD ALWTELKTLY PISITIDEVI
     TEAGSKGRVN RDFVRREILS DAKLAYSKRE EQLGGAAMRE LERRVVLSVI DRRWREHLYE
     MDYLKDGIGL RAMAQRDPLV EYQREGFALF QQMMGAIREE TVGFLFNLEV EVQAPADAES
     VGPRIQAKGL AANQATADKL RYTAPTDDGG VEVRNQRGQI EKAATAKAQK DQQAEDAVLV
     GEDEPETPQG PPARGAFGQP TGASSSAPQN REERRKADRR K