SECA_MYCMS
ID SECA_MYCMS Reviewed; 944 AA.
AC Q6MUE3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=MSC_0089;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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; BX293980; CAE76741.1; -; Genomic_DNA.
DR RefSeq; NP_975099.1; NC_005364.2.
DR AlphaFoldDB; Q6MUE3; -.
DR SMR; Q6MUE3; -.
DR STRING; 272632.MSC_0089; -.
DR EnsemblBacteria; CAE76741; CAE76741; MSC_0089.
DR KEGG; mmy:MSC_0089; -.
DR PATRIC; fig|272632.4.peg.92; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_1_14; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001016; 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..944
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320858"
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; 107797 MW; D5ABD744ACF2FA3D CRC64;
MVSDRRLLKK FGKIADKIIA LEPQMRQLKD EDFILKTQEF KQMLENGKSL DDILIEVYAV
AREAARRVLG LNAYKMQLIG GIILNSGDIA EMRTGEGKTL TGIFPAYLNA LSGKGVHIVT
VNEYLSRRDS EINGKVFDLL GISVGLNGSS LTKTEKREAY NKDITYTTNA ELGFDYLRDN
MVSDYSLKVQ RKLNYCIIDE ADSVLIDEAR TPLIISGGTS TRINLYKAAN NFALTLKEHD
DLDIDLESKQ VYLNEQGMKK ANEFFSLKNL FAIENTEIFH LIMNALKAQF AFKEGVEYTV
RDNEILLIDQ FTGRIMHGRS YSDGLQQALQ AKENVDIEEE TVTLATITYQ NFYRLYSKIA
GMTGTAKTEE EEFIKIYNTR VIQTPTNKPV IRKDEPDLTF GTKNAALKKL VEDVLEAHKK
GAPILIGTTS VESSEQIARY LKKANLKFET INAKNHDREA EIVAKAGEIG AITLATNMAG
RGTDIKLAKG VAELGGLRVF GVERNEARRI DNQLRGRSGR QGDPGLSRFY ISMDDDLMMR
FTAPKTRQRF KALGDDYIKS KMFTRAVTNA QKKLEGMNFD QRKNVLDYDN ILAQQREIIY
AQRDDILEAN DLSVVIEKMQ ITAAYELIEK HSTLVHGEKT INKKELLEVI DGILVPKNKF
RIDDFNNKEK MDLAVEIAEA MMQLYKARIS DIPDDVIIVM ERKIILDAFD KHWTKHLDIA
GKLKSGIYLQ QYAQNNPLAI YIEQATNLFN KMKINIANEV VENLANVILR VVEDEEQREE
RIEVTDKDIE EILFETGLQP SDINNKAINQ RFDELEEEFK DDKQKLRRLR IQRDVMLGLV
LELERRAEMI ISPQNDQQAI TQLIKELQND IDIASITIDQ IHQNFNNMVE QINDPEKLKH
LVIAKDVLLQ LVARMDDIKE QEKQTRKKKK KKPHEDESSK TKIG
