GYRA_TREPA
ID GYRA_TREPA Reviewed; 813 AA.
AC O83051;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=TP_0005;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC64998.1; -; Genomic_DNA.
DR PIR; D71378; D71378.
DR RefSeq; WP_010881455.1; NC_021490.2.
DR AlphaFoldDB; O83051; -.
DR SMR; O83051; -.
DR IntAct; O83051; 9.
DR STRING; 243276.TPANIC_0005; -.
DR EnsemblBacteria; AAC64998; AAC64998; TP_0005.
DR KEGG; tpa:TP_0005; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_12; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000811; 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..813
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145271"
FT MOTIF 531..537
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 813 AA; 89926 MW; 1F6A3AE08C43ECC4 CRC64;
MEEISTPEGG VLVPISIETE VKRAYIDYSM SVIVSRALPD VRDGLKPVHR RILYAMEEKG
LRFSGPTRKC AKIVGDVLGS FHPHGDASVY DALVRLGQDF SLRYPVIHPQ GNFGTIGGDP
PAAYRYTEAK MARIAESMVE DIKKETVSFV PNFDDSDVEP TVLPGRFPFL LANGSSGIAV
GMTTNMPPHN LREIAAAISA YIENPNLSIQ ELCDCINGPD FPTGGIIFGK NGIRQSYETG
RGKIVVRARF TIETDSKGRD TIIFTEVPYQ VNTTMLVMRI GELARAKVIE GIANVNDETS
DRTGLRIVVE LKKGTPAQVV LNHLFAKTPL QSSFNVINLA LVEGRPRMLT LKDLVRYFVE
HRVDVVTRRA HFELRKAQER IHLVRALIRA LDAIDKIITL IRHSQNTELA KQRLREQFDF
DNVQAQAIVD MQMKRLTGLE VESLRTELKD LTELISSLEE LLTSPQKVLG VVKKETRDIA
DMFGDDRRTD IVSNEIEYLD VEDFIQKEEM VILISHLGYI KRVPVSAYRN QNRGGKGSSS
ANLAAHDFIS QIFTASTHDY VMFVTSRGRA YWLKVYGIPE SGRANRGSHI KSLLMVATDE
EITAIVSLRE FSNKSYVFMA TARGVVKKVT TDNFVNAKTR GIIALKLSGG DTLVSAVLVQ
DEDEVMLITR QGKALRMSGR EVREMGRNSS GVIGIKLTSE DLVAGVLRVS EQRKVLIMTE
NGYGKRVSFS EFSVHGRGTA GQKIYTQTDR KGAIIGALAV LDTDECMCIT GQGKTIRVDV
CAISVLGRGA QGVRVLDIEP SDLVVGLSCV MQG
