ID SECA_MYCGA Reviewed; 890 AA.
AC Q7NC50;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=MYCGA0310;
GN ORFNames=MGA_0670;
OS Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasma gallisepticum).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; AE015450; AAP56381.1; -; Genomic_DNA.
DR RefSeq; WP_011113260.1; NC_004829.2.
DR AlphaFoldDB; Q7NC50; -.
DR SMR; Q7NC50; -.
DR KEGG; mga:MGA_0670; -.
DR PATRIC; fig|233150.7.peg.33; -.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000001418; 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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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 NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 2.
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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of 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..890
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320853"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
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 890 AA; 101679 MW; C19D4A9156A120E6 CRC64;
MLINWFKLIS PKNRILKRAT LAAKQVDALK DEMRALSDEQ LFNKTEYFIN ELKNNKTTDD
ILVEAFAVIR EVVYRETGNF AYLVQLIGAY VVHQGDFSEM MTGEGKTLTL VLAAYLNMLE
KKGVHIVTVN EYLAERDAEQ ARRIFARLNL TVGCNKANLA PHLKKEAFDC DLTYTTNSEL
GFDYLRDNMV RNYRDKKIRG LHFAIVDEGD SILIDEARTP LIISGQPKKD FRMYFDADKF
VETLSESDYK IDPESRSPSL TEKGITKAEK HFKINNLFDL ENSDLFHKIG NALTARKIFQ
NGKEYIVRDD KILIVDHFTG RILEGRSYNG GLHQAVQAKE RVPIEAENVV VATVTYQSFF
RMYKKLAAVS GTALTESEEF LKIYNMVVVP VPTNRPVIRK DHPDFMFGNL KTKWEAVVNE
IEKIHKTGQP ILVGTGSVED SETLHQMLLE KNIMHEVLNA KNHAREAHII AKAGEVGSVT
ISTNMAGRGT DIKLGKGAKE LGGLYVIGTE RHESRRIDNQ LRGRSGRQGD IGESRFFISF
GDPLFKRFAQ DRILKAQEKL ASDYFDSKFF SRFLTMTQKK VESVNFDMRK NLIDYDHVLA
NQRELIYKQR DKILIASDLT EVVDRMAQNF VEGFVETFKD QANQTMVNPI ELSIAVQKEL
LQGEEVTASQ FYNQTLLAAK QTVLKLVKDA ISKKIEVMTV GIANNVFRDI IIQQMDDAWI
HHLDQMLKLR EGVSLRSLEQ TSPLNIYVEE SKKLFDLMLN KIAKNVILAV CAIINPTRNV
DINVEQEHRR LEALKRLEEI KKLEELQNNN NEPAKVLFKF PDQHGNMIER EVPVDNLIQL
VDGQIIQAQV AEEPKQELNQ LEKADQLDQT LIEAKLAEQQ EQKNNSATDK
//
