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GYRA_MYCPN
ID   GYRA_MYCPN              Reviewed;         839 AA.
AC   P22446; P75108;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=MPN_004;
GN   ORFNames=MP150;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
RX   PubMed=2172693; DOI=10.1111/j.1365-2958.1990.tb00687.x;
RA   Colman S.D., Hu P.C., Bott K.F.;
RT   "Mycoplasma pneumoniae DNA gyrase genes.";
RL   Mol. Microbiol. 4:1129-1134(1990).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=11271496;
RX   DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA   Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA   Frank R.;
RT   "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL   Electrophoresis 21:3765-3780(2000).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       modulate DNA topology and maintain chromosomes in an underwound state.
CC       Negative supercoiling favors strand separation, and DNA replication,
CC       transcription, recombination and repair, all of which involve strand
CC       separation. Also able to catalyze the interconversion of other
CC       topological isomers of dsDNA rings, including catenanes and knotted
CC       rings. Type II topoisomerases break and join 2 DNA strands
CC       simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01897};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC       the heterotetramer, GyrA contains the active site tyrosine that forms a
CC       transient covalent intermediate with DNA, while GyrB binds cofactors
CC       and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II topoisomerases;
CC       in organisms with a single type II topoisomerase this enzyme also has
CC       to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR   EMBL; U00089; AAB95798.1; -; Genomic_DNA.
DR   EMBL; X53555; CAA37623.1; -; Genomic_DNA.
DR   PIR; S73476; S73476.
DR   RefSeq; NP_109692.1; NC_000912.1.
DR   RefSeq; WP_010874361.1; NC_000912.1.
DR   AlphaFoldDB; P22446; -.
DR   SMR; P22446; -.
DR   IntAct; P22446; 6.
DR   STRING; 272634.MPN_004; -.
DR   EnsemblBacteria; AAB95798; AAB95798; MPN_004.
DR   KEGG; mpn:MPN_004; -.
DR   PATRIC; fig|272634.6.peg.4; -.
DR   HOGENOM; CLU_002977_6_1_14; -.
DR   OMA; THHWLLF; -.
DR   BioCyc; MPNE272634:G1GJ3-7-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
FT   CHAIN           1..839
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145241"
FT   MOTIF           537..543
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        134
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   839 AA;  93357 MW;  C499618577714AFE CRC64;
     MAKQQDQIDK IRQELAQSAI KNISLSSELE RSFMEYAMSV IVARALPDAR DGLKPVHRRV
     LYGAYTGGMH HDRPFKKSAR IVGDVMSKFH PHGDMAIYDT MSRMAQDFSL RYLLIDGHGN
     FGSIDGDRPA AQRYTEARLS KLAGELLRDI DKDTVDFVAN YDGEEQEPTV LPAAFPNLLA
     NGSSGIAVGM STSIPSHNLS ELIQGLILLI DNPDCTINDL LGVIKGPDFP TGANIIYTKG
     IESYFETGKG NVVIRSKVSI EQLPTRAALV VTEIPYMVNK TSLIEKIVEL VKAEEITGIA
     DIRDESSREG IRLVIEVKRD TVPEVLLNQL FKSTRLQVRF PVNMLALVKG APKLLNMKQA
     LTVYLEHQLD VLIRKTQFNL KKYQERFHIL SGLLIAALNI DEVIAIIKKS ANNQVAMEAL
     HERFGLDEIQ ARAVLDMRLR SLSVLEVNKL QTEQQELKAL IEFCQQVLAD KQLQLKLIKE
     QLTKINEQFG DPRRSEILYG ISEDIDDEDL ITQENVVITM STNGYLKRIG VDAYNLQHRG
     GVGVKGLTTY TDDSISQLLV CSTHSDLLFF TDKGKVYRIR AHQIPPGFRT NKGIPAVNLI
     KIDKDEKICA LISVNDYQNG YFFFCTKNGT IKRTSLSEFA NILSIGKRAI LFKENDVLFS
     VIRTSGQDDI FIGSTAGFVV RFHEDTVRPL SRAAMGVLGI NLNQCEFVNG LSTSSNGSLL
     LSVGQNGIGK LTSIDKYRLT KRNAKGVKTL RVTAKTGPVV TTTTVFGNED LLMISSAGKI
     VRISLEQLSE QRKNTSGVKL IKLKEKERLE TVTIFKKEEA IKTTTATETD DVGSKQITQ
 
 
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