SECA_MYCMO
ID SECA_MYCMO Reviewed; 854 AA.
AC Q6KIK4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=MMOB0860;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(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; AE017308; AAT27572.1; -; Genomic_DNA.
DR RefSeq; WP_011264606.1; NC_006908.1.
DR AlphaFoldDB; Q6KIK4; -.
DR SMR; Q6KIK4; -.
DR STRING; 267748.MMOB0860; -.
DR EnsemblBacteria; AAT27572; AAT27572; MMOB0860.
DR KEGG; mmo:MMOB0860; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000009072; 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; -; 3.
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..854
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320857"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 99..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 854 AA; 98101 MW; C5AFACB56B13F5E7 CRC64;
MKFLKNIKSL EFRLAESMLK SINDLKEKYL AFSDEELKNM TNVFKEKLKK NVSLESIRID
AFAVAREATF RVLKKRPYDV QMIGGLILDF GSVAEMKTGE GKTITSIAPV YLNALKGSGV
IVSTVNEYLA ERDAAEMGEV FKWLGLSVGL NKANMPSNLK RAAYKCDITY SVHSELGFDY
LRDNMVNSFE EKVQRDLNFA LIDEVDSILI DEAKTPLIIS GGKSDEVSLY AVTDQFVRTL
DHVDYAIDEE TKAINLTAQG IEKTKKFFNF NSLYNLENSE LIHRLQNALR AHKVMKKDVE
YVVLNGKIEL VDTFTGRIME GRSYSEGLQQ AIQAKELVEI DPETKTLATI TYQNFFRLFK
KLSGMTGTGK TEEQEFIDIY NMRVTEIPTN VPIARIDHPE KVYVTFQAKY KAVVEEIKRL
HAKKQPILVG TSQVEESEYL HQLLLKENLP HTVLNAKQNK NEADIIAKAG IAGAITIATN
MAGRGTDIKP DAESLKQGGL FVLGTDKSEA RRIDNQLKGR SGRQGDVGES RFFISIDDQL
IRRFSLQDKW KEIFAEYKDN EIIDKQIKKA FDKAQRKIEG FNYDNRKNVL NYDDVIRQQR
DIIYSQRDSI LLQDDLSLVV EKMIQRNSKQ IIKYGELYTR TGALDHKALV NFVNKEYMNI
CDFKFTLEDF NNYINEEIPQ HLSNILIREY RKMREFLVEK SGKLPTNLFE RRAIISALDE
KWQNHINLMD KLRQSVNLVQ YSQKNPFQTY TEIGTKHFEQ LVEDIATNSL KIIMNNPSAK
FQNLDGDFKN EQIKLEDGSI ITIPANIPFD IKEQIISKAK ELLKESGEKR KVFEKNILSD
LNLVDEKFRD SSKW
