ID V4PTL1_9CAUL Unreviewed; 934 AA.
AC V4PTL1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=ABENE_12040 {ECO:0000313|EMBL:ESQ90694.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ90694.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ90694.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ90694.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ90694.1}.
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DR EMBL; AWGB01000022; ESQ90694.1; -; Genomic_DNA.
DR RefSeq; WP_018079982.1; NZ_AWGB01000022.1.
DR AlphaFoldDB; V4PTL1; -.
DR STRING; 1121022.GCA_000376105_00304; -.
DR PATRIC; fig|1121022.4.peg.2441; -.
DR eggNOG; COG0188; Bacteria.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000017837; Unassembled WGS sequence.
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:UP000017837};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 32..511
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 572..578
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 143
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 934 AA; 101505 MW; FDFAD7D32EA2A50B CRC64;
MNDTTSYESL GPDDQEPGQG SGGQPPAGIS FVTIEDELKR SYLDYAMSVI VSRALPDARD
GLKPVHRRIL YSMHQLGMQP SKSYSKCARV VGDVLGRFHP HGDASVYMAL VRMAQPFSMG
LMLIDGQGNF GSVDGDMPAS MRYTECRMAT SAAALLADIE QDTVDFQPNY DGKEEEPTVL
PARIPNLLVN GAGGIAVGMA TNIPPHNLGE IVDACVAMLD NPAITLEELL DIVPGPDYPT
GGEILGRTAA RNALMTGRGS VVTRGKATIE TLRKDREGIV ITELPYQVNK ATLTEYIADM
VREKRIEGIS DIRDESDRDG MRMVIELKRE ASGDVILNQL YRYTALQSSF GVNMLALNHG
RPQQMGLRQL LDIFLEFREE VVVRRTRFEL NKARDRGHVL VGLTIAVANI DEVIHIIRSS
ADPAEARDRL TQRVWPAGDM APLIDLIADP RSIVMADSSV RLTDEQARAI LALTLSRLTG
LGRDEIGTEA RALADAIAGY LEILGSRERI VGIIREELLE VRAQFAVPRR TTILDGEGDI
EDEDLIPREE MVVTVTHSGY VKRTALAAYR EQHRGGKGRS GMAMKDEDAI IGVYSATTHQ
PMLFFSSTGK AYKLKVWRLP LGNPQSKGKA FVNLLPLDSG ETITNILALP EDEAAWERQD
IIFATRSGDI RRNKLSDFVN VNRAGKIAMK LEDGDTIVGV AVCNEDQDVL LSTAGGRSIR
FAVDEVRVFK GRDSTGVRGV RLAGEDTVIS MAILRRVDAT PAERAAYLKY AAQQRAALAS
SEEGDDAVVV AVEESEDEGD VGEANLTPER IAELTAAEEF ILTVADTGFG KRTSSYDYRR
TGRGGQGIVA IDLSKRGGKL AASFPIDATD GLLLVTSGGQ LIRTNVTTVR IASRNTQGVT
IFRTSGGEKV VSVERIVDSG DDEANEGAVS GEQT
//
