SECA1_MYCVP
ID SECA1_MYCVP Reviewed; 938 AA.
AC A1T5Y4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Mvan_1762;
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; ABM12584.1; -; Genomic_DNA.
DR RefSeq; WP_011779003.1; NC_008726.1.
DR AlphaFoldDB; A1T5Y4; -.
DR SMR; A1T5Y4; -.
DR STRING; 350058.Mvan_1762; -.
DR PRIDE; A1T5Y4; -.
DR EnsemblBacteria; ABM12584; ABM12584; Mvan_1762.
DR KEGG; mva:Mvan_1762; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
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; 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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..938
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318393"
FT REGION 865..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 102..106
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 938 AA; 104771 MW; 47F30CB7D5CB65C7 CRC64;
MLSKLLRLGE GRMVKRLKGV ADYVNTLSDD IEKLSDAELR GKTDEFRARL AGGKEDLDDV
MPEAFAVVRE AAWRVLNQRH FDVQIMGGAA LHFGNVAEMK TGEGKTLTSV LPAYLNALPG
KGVHIVTVNE YLAKRDAEQM GRVHRFLGLD VDVILGTLTP DQRRAAYNAD ITYGTNWELG
FDYLRDNMAL RLEDCVQRGH HFAIVDEVDS ILIDEARTPL IISGPADGGS NWYTEFARLA
PLMKPDVHYE VDIKKRVVGI NEAGVEFVED QLGIENLYEA ANSPLISYLN NAIKAKELFE
RDKHYIVRNG EVFIVDEFTG RMLVGRRYNE GLHQAIEAKE HVEIKAENQT VAQVTLQNYF
RMYEKLAGMT GTAETEAAEL HEIYKLGVVP IPTNRPMVRK DQSDLIYKTE EAKYIAVVDD
VAERYEKGQP VLIGTTSVER SEFLSRQFEK RRIPHNVLNA KYHEQEAGIV AEAGRLGAIT
VATNMAGRGT DIVLGGNVDY LLDRRLRQRG LDPIETPEEY EQGWHEELPH IKAEVAAEAK
DVIAAGGLYV LGTERHESRR IDNQLRGRSG RQGDPGESRF YLSLADELMR RFNGATLETL
LTRLNLPDDV PIEAKMVSRA IKSAQTQVEQ QNFDIRKEVL KYDEVMNQQR KVVYAERRRI
LEGENLAGQA HQILVDVITA YVDGATAEGY SEDWDLEKLW EGLRQLYPVG IDHHDLIDSD
AVGEPGELTR EELLQALIAD AERAYAAREA EIEEIAGEGA MRQLERNVLL NVLDRKWREH
LYEMDYLREG IGLRGLAQQR PEVEYAREGY DMFIAMLDGM KEESVGFLFN VQVERAPSAP
TVAAQAAPAG LAAFAAAAAE QAQAQTGGVA TKERPAVGGL RAKGIDDKAQ PLTYTGPSED
GGVEVKRSGG GTPSTGGTRK ERREAARQQK TGRHAKRR
