ID Q165T2_ROSDO Unreviewed; 905 AA.
AC Q165T2;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897,
GN ECO:0000313|EMBL:ABG32261.1};
GN OrderedLocusNames=RD1_2726 {ECO:0000313|EMBL:ABG32261.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32261.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG32261.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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DR EMBL; CP000362; ABG32261.1; -; Genomic_DNA.
DR AlphaFoldDB; Q165T2; -.
DR STRING; 375451.RD1_2726; -.
DR KEGG; rde:RD1_2726; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR Proteomes; UP000007029; 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; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000007029};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 13..492
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 553..559
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 124
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 905 AA; 100069 MW; 86CA057720C91B68 CRC64;
MRPERPVYDG PSVSIEQEMR TSYLDYAMSV IVSRAIPDLR DGLKPVHRRI LFAMHETGNT
HDKPYRKSAR PVGDVMGQYH PHGDSAIYDA LVRMAQDFSM SLPLLDGQGN FGSMDGDNPA
AMRYTEVRMD KPAAYLLADI DKDTVDFQDN YDGKQKEPTV LPARFPNMLV NGAGGIAVGM
ATNIPPHNLG EVIDATLALI EEPDLTSEQL IDYVPGPDFP TGGIMLGRGG ARKAYLEGRG
SVIIRAKTRV EEIRKDRWAI IVDEIPYQVN KATMIEKIAE QVREKKIDGI AHVQDESDRN
GVRVVIELKR DATAEVVMNQ LYRFTPLQTY FGCNMLALNG GRPEQLTLRK FLTYFIDFRE
DVVARRTAYL LRKARERSHV LCGLAVAVTN IDEVVATIRA SADAAEAREK LMTRRWPAQD
ILPYIALIDD PTHTANDDGT YNLSETQARA ILDLRLQRLT QIGVKEVTDE LEELAGKIKE
YLEILGSRDR IMGIIADELR EVRELFAVPR RTEIVDWSGD MEDEDLIARE DMVVTVTQGG
YIKRTPLADF RSQRRGGKGL SGGSLKEDDV VTTLFVANTH TQLLFFTTDG MAYKLKTWRL
PQGARTSKGK AIVNILPIPQ GVSIAAILPI DRDEKDWSQL QIVFATSAGT VRRNALSDFT
NVKSNGKIAM KFEDEHAETT LINARIASPD DDVMLVTASG RAIRFPSEDV RVFNSRSSVG
VRGVKLSGHD KVVSMSVIRH FDATADERAA YLKMRRAMVG LTDDSETSDE DETSANATIS
PDRYAEMSAA ENLILTLTAG GAGKLSSSHD YPVRGRGGMG VTAWDKRMQT GQIVASFPVE
MDDQIMLATS KGQSIRVPVE GISFRSRSAG GVKVFNTGKG EEVVSVAWIA DQGEDDTDGE
DAQNA
//
