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