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SECA2_MYCVP
ID   SECA2_MYCVP             Reviewed;         850 AA.
AC   A1T5H7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Mvan_1598;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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; CP000511; ABM12427.1; -; Genomic_DNA.
DR   RefSeq; WP_011778852.1; NC_008726.1.
DR   AlphaFoldDB; A1T5H7; -.
DR   SMR; A1T5H7; -.
DR   STRING; 350058.Mvan_1598; -.
DR   EnsemblBacteria; ABM12427; ABM12427; Mvan_1598.
DR   KEGG; mva:Mvan_1598; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_2_11; -.
DR   OMA; SHTIGME; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000009159; 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; 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; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Translocase; Translocation;
KW   Transport.
FT   CHAIN           1..850
FT                   /note="Protein translocase subunit SecA 2"
FT                   /id="PRO_0000318395"
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         491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   850 AA;  95399 MW;  EB72219D2E3BB058 CRC64;
     MLADVLRLGE ARTVKQLSAI ADHVDSLARG VENLTDAELS SRTDVFRRRV ADGDVLDELL
     PEGFAVAREA AWRVLGLRPY HVQVMGGAAL HFGNIAEMMT GEGKTLACVM PAYLNAIGGK
     GVHIVTVNDY LAGRDAEQMG RVHRFLGLTV GVILSEMKPD ERRAAYAADI TYGTNNEFGF
     DYLRDNMAGR LEDRVQRGHC YAIVDEVDSI LIDEARTPMI ISGPADDATR WYAEFARLAA
     LMTRDVHYEV DTRRRTIGVS EAGVALVEDQ LGVDNLYQVV HAPLVGHLNN AVRAKELFHR
     DREYIVNDDG EVLIVDEFTG RVLVGRRYNE GLHQAIEAKE GVEVKPENQT LATITLQNYF
     RLYDRLAGMT GTARSEASEF RDIYRLGVIT IPPNRPVVRR DEVDVVYKTE SAKFDAVVED
     VVGRHAAGQP VLIGTTSVEK SEYLSGRLTE RRVPHTVLNA KHLEQEAAIV AEGGRRGAVT
     VATDMAGRGT DIMLGGNVDF LTDKRLRSRG LHPTRSPEEY DAAWAEVRRE VAAESRTEAR
     EVVALGGLYV LGTERHESRR IDNQLRGRSG RQGDPGETRF YVSLCDELMR RSATFDLEKL
     MSRLKMPERE PIEAKVVSRA IRNAQSQVEQ ANFDMRRSVV KYGQVLDQQR RIVYQARSRL
     LEGEDMQHQI FHMIGDVVTA YVNECTAGRR TADWDLETLR AALSTLYPVV WQPDPRPHMR
     GLTRSVLRHE VIADARRALV RRKAAIEARS GLRVMRELER AILLDCLDSK WRAHLYEMDY
     LAAGIGMRAL AGADPVVEYH REGHRMFVRM LEAVKEQSIR SLFDATTRML APIMPSAARS
     PGTPDPRWPF
 
 
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