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SECA2_MYCPA
ID   SECA2_MYCPA             Reviewed;         777 AA.
AC   Q73ZR7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=MAP_1534;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03851.1; -; Genomic_DNA.
DR   RefSeq; WP_003877905.1; NC_002944.2.
DR   AlphaFoldDB; Q73ZR7; -.
DR   SMR; Q73ZR7; -.
DR   STRING; 262316.MAP_1534; -.
DR   EnsemblBacteria; AAS03851; AAS03851; MAP_1534.
DR   KEGG; mpa:MAP_1534; -.
DR   PATRIC; fig|262316.17.peg.1625; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_2_11; -.
DR   OMA; WADHLAF; -.
DR   Proteomes; UP000000580; 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; IPR026389; SecA_Actinobact_type.
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; 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; TIGR04221; SecA2_Mycobac; 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..777
FT                   /note="Protein translocase subunit SecA 2"
FT                   /id="PRO_0000318381"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         112..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   777 AA;  85031 MW;  4F1ABC900ABB6872 CRC64;
     MPKTNRAQPG RLSSRFWRLL GASTEKNRSR SLTLVTDSSE YDDEAAGLTD EQLRKAAGLL
     NLEDLAESED IPQFLAIARE AAERATGLRP FDVQLLGALR MLAGDVIEMA TGEGKTLAGA
     IAAAGYVLAG RHVHVVTIND YLARRDAEWM GPLIEAMGLT VGWITAESSS EERRAAYGCD
     VTYASVNEIG FDVLRDQLVT DVADLVSPNP DVALIDEADS VLVDEALVPL VLAGTTHRET
     PRLEIIKLVG ELEAGTDYDT DADSRNVHLT DVGARKVEKA LGGIDLYSEE HVGTTLTEVN
     VALHAHVLLQ RDVHYIVRDD AVHLINASRG RIAQLQRWPD GLQAAVEAKE GIETTETGEV
     LDTITVQALI NRYATVCGMT GTALAAGEQL RQFYKLGVSP IPPNKPNIRE DEADRVYITA
     AAKNDAIVEH IIEVHETGQP VLVGTRDVAE SEELHERLLR RGVPAVVLNA KNDAEEAQVI
     AEAGKFGVVT VSTQMAGRGT DIRLGGSDEA DHDRVAELGG LHVVGTGRHH TERLDNQLRG
     RAGRQGDPGS SVFFSSWEDD VVAANLDRNK LPMETDPETG DGRIVSPKAA GLLDHAQRVA
     EGRMLDVHAN TWRYNQLIAQ QRAIIVDRRN TLLRTATARE ELAELAPKRY RELADEIPEE
     RLETICRHIM LYHLDRGWAD HLAYLADIRE SIHLRALGRQ NPLDEFHRLA VDAFASLAAD
     AIEAAQQTFE TANVLEDEPG LDLSKLARPT STWTYMVNDN PLSDDTLSTL SLPGVFR
 
 
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