SECA_METSB
ID SECA_METSB Reviewed; 949 AA.
AC B8EM60;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Msil_2525;
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX PubMed=20472789; DOI=10.1128/jb.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK51449.1; -; Genomic_DNA.
DR RefSeq; WP_012591518.1; NC_011666.1.
DR AlphaFoldDB; B8EM60; -.
DR SMR; B8EM60; -.
DR STRING; 395965.Msil_2525; -.
DR PRIDE; B8EM60; -.
DR EnsemblBacteria; ACK51449; ACK51449; Msil_2525.
DR KEGG; msl:Msil_2525; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_5; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002257; 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; 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..949
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184240"
FT REGION 852..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..939
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 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 933
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 944
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 945
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 949 AA; 105845 MW; 503B29BBAC13ACF4 CRC64;
MLGSFAKKIF GSANERRLKS YRPKVAAINA LEPEWLKLSN EELAAKTVAF REELAQGKSL
DDLLVPAFAT VREAARRVLG QRHFDVQLIG GMVLHEGAIA EMRTGEGKTL VATLATYLNA
LAGKGVHVIT VNDYLARRDA EWMGRVYQFL GLTTGIIVHG VDDGERARSY AADITYGTNN
EFGFDYLRDN MKYELSQMVQ RGHSFAIVDE VDSILIDEAR TPLIISGPSD DKSELYNTID
KVMPRLQPED FEVDEKQRST NLTERGNEHI EDLLRAAGVE IEGSLYEAAN VTIVHHVNQA
LRAHKLFQRD KDYIVRNGEV VIIDEFTGRM MPGRRYSEGL HQALEAKEHV QVQPENVTLA
SITFQNYFRL YSKLAGMTGT ASTEADEFAE IYKLDVVDIP TNLPVCRLDE DDEVYRSAEE
KLRAIVREIE AANAKMQPML VGTTSIEKSE QLAEAMKSHG YKQIDFAEPR ALDKLYAAAR
AEKPSKLFAV LNARFHEQEA YIVAEAGVPG AITIATNMAG RGTDIKLGGN VDMRVAQECA
DLEPGEARDA KDAQIRAEVD DFKAKAIAAG GLYIIGTERH ESRRIDNQLR GRAGRQGDPG
RSKFFLSLKD DLMRIFGSDR MESMLVKLGL KEDEAIVHSW INKALEKAQQ KVEARNFDMR
KNILKYDNVM NDQRKVVFEQ RREMMAKPSL EEMIDDMRQG VVDDLIARHI PRDAYPEAWD
SEGLREGVKT SLNIDLPIVE WAKEEGITED DMRERLQKAA DEAYAARVER NGVDVTRYVE
KQIVLQALDH LWREHLLTLD HLRQVVGWRG MAQRDPLNEY KSEAFQLFDE LIAQLREATT
AQLSRVEVAF EPPPGENGFS GGMQEISGPQ GGSSGGPIFQ EALSAAAFAP PPLAPLEFSD
ESGSTATLAR PAQSASRDEP AGGYAKVGRN QPCPCGSGKK YKHCHGALT
