ID A0A0M4D9W9_SPHS1 Unreviewed; 915 AA.
AC A0A0M4D9W9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=LH20_09870 {ECO:0000313|EMBL:ALC12257.1};
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC12257.1, ECO:0000313|Proteomes:UP000061305};
RN [1] {ECO:0000313|EMBL:ALC12257.1, ECO:0000313|Proteomes:UP000061305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113P3 {ECO:0000313|EMBL:ALC12257.1,
RC ECO:0000313|Proteomes:UP000061305};
RX PubMed=26472829;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT Sphingopyxis sp. 113P3 (NBRC 111507).";
RL Genome Announc. 3:e01169-15(2015).
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; CP009452; ALC12257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4D9W9; -.
DR STRING; 292913.LH20_09870; -.
DR KEGG; sphp:LH20_09870; -.
DR PATRIC; fig|292913.6.peg.1992; -.
DR Proteomes; UP000061305; 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:UP000061305};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 18..502
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 891..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 563..569
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 129
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 915 AA; 100153 MW; 26F133FE077179EE CRC64;
MTEENTPMQP SEDGVSPINI VDEMKTSYLD YAMSVIVSRA LPDVRDGLKP VHRRILYAAQ
EGGFVPGRPY KKSAKIVGDV MGNYHPHGDS AIYDALARMT QDWSLRVPLI DGQGNFGSMD
PDPPASMRYT EARLAKTAMV LLNDLDKDTV DFQPNYDASR EEPTVLPARF PNLLVNGAGG
IAVGMATNIP PHNLGEVVDA TLAMIDRQLE GGADITLEEL MAIVPGPDFP TGAMMLGQGG
ARNAYATGRG SIMMRATHVI EEGRNDRQSI VLTSIPFQVG KSGLVEKIAE AARDKRIEGV
ADIRDESNRE GVRVVIELKR DATAEVVLNQ LWRHTPAQSS FPANMLAIRG GRPEMLGLKD
ILSSFIAFRE DVITRRCKFE LAKARDRAHI LLGLVVAVSN LDEVVRIIRG ASNPAAAREA
LLAREWPIGE IAPYIRLVEA IEGEMEESAV YRLSETQVKA ILDLRLHRLT ALGRDEIGKE
LEELAAEIEE LLSILADRVK LYGVMREELV AVRDEFATPR KTIVAPAADG IDDEDLIERE
EMVVTVTLDG YIKRTPLETF RAQRRGGKGR AGMATKDEDV VTNLFVTSTH TPVLFFSTAG
KVYRLKVWRL PEGGPATRGR PMVNLLPLAQ GETISTVLPL PEDEAEWGKL HVMFATAKGN
VRRNSMDAFT NVPSNGKIAM KFEGEDEDDR LIGVALLGEN DDVLLATRQG KAIRFAGDEV
REFQSRNSTG VRGMKLAKND DEVISLSILH RGGMRDQEER EDYLRFAPWK AEKEGAPKMS
DERFAELAGR EQFILTVCAN GYGKLSSAYE YRRTGRGGQG ITNIDNIRRN GPVVASFPAT
QAHQLMLVTD QAKLIRMGLD TLRVIGRGSA GVRLFDVAEG EHVVSAALIE ESEDGAPDEG
AASEVAAAAG ETGGE
//
