SECA_MYCCT
ID SECA_MYCCT Reviewed; 944 AA.
AC Q2ST71;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=MCAP_0045;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) 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; CP000123; ABC01329.1; -; Genomic_DNA.
DR RefSeq; WP_011386947.1; NC_007633.1.
DR AlphaFoldDB; Q2ST71; -.
DR SMR; Q2ST71; -.
DR TCDB; 3.A.5.3.1; the general secretory pathway (sec) family.
DR PRIDE; Q2ST71; -.
DR EnsemblBacteria; ABC01329; ABC01329; MCAP_0045.
DR GeneID; 23779000; -.
DR KEGG; mcp:MCAP_0045; -.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR PhylomeDB; Q2ST71; -.
DR Proteomes; UP000001928; 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; Translocase; Translocation; Transport.
FT CHAIN 1..944
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320852"
FT REGION 920..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 95..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 944 AA; 107682 MW; 191601AB60ED1478 CRC64;
MVSDRRLLKK FGKIADRIIA LEPQMRQLKD EDFLLKTQEF KQMLENGKSL DDILIEVYAV
AREAARRVLG LNAYKVQLIG GIILNSGDIA EMRTGEGKTL TGIFPAYLNA LTQKGVHIVT
VNEYLSRRDS EINGKVFDLL GISVGLNGSS LSKAEKREAY SKDITYTTNA ELGFDYLRDN
MVSDYSLKVQ RKLNYCIIDE ADSVLIDEAR TPLIISGGTS TRINLYKAAN NFALSLKEHD
DLDIDLESKQ VYLNEQGMKK ANEFFSLKNL FAIENTEIFH LIMNALKAQF AFKEGVEYTV
RDNEILLIDQ FTGRIMHGRS YSDGLQQALQ AKENVDIEEE TVTLATITYQ NFYRLYSKIA
GMTGTAKTEE EEFIKIYNTR VIQTPTNKPV IRKDEPDLTF GSKNAALKKL VEDVKETHQK
GAPILIGTTS VESSEQIARY LKKANLKFET INAKNHDREA EIVAKAGEIG AITLATNMAG
RGTDIKLAKG VSELGGLRVF GVERNEARRI DNQLRGRSGR QGDPGLSRFY ISMDDDLMMR
FTAPKTRQRF KALGDDYIKS KMFTRAVTNA QKKLEGMNFD QRKNVLDYDN ILAQQREIIY
AQRDDILEAN DLSIVIEKMQ ITAAYELIEK HSTLVHGEKT INKKELLEVI DGVLVPKNKF
RIDDFNNKEK MDLAVEIAEA MMQLYKARIS DIPEDVVIGM ERKIILDAFD KYWTKHLDIA
GKLKSGIYLQ QYAQNNPLAI YVEQATDLFN KMKINIANDV VENLSNVILK VVEDEEKREE
RIEVTDKDIE EILLETGLET SDINNKAINK RFDELEEKFK DDKQKLKRLR IQRDVMLGLV
LELERRAEMI VSPENDQLAI TQLIKELQND IDIASITVEQ IHQNFNNMVE KINDPEKLKH
LVIAKDVLLQ LVARMDDIKE QEKQTKKKKK KKPHDDETTK VKIG
