ID A0A495RG16_SPHMI Unreviewed; 904 AA.
AC A0A495RG16;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=DFR51_3148 {ECO:0000313|EMBL:RKS86442.1};
OS Sphingosinicella microcystinivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Sphingosinicella.
OX NCBI_TaxID=335406 {ECO:0000313|EMBL:RKS86442.1, ECO:0000313|Proteomes:UP000276029};
RN [1] {ECO:0000313|EMBL:RKS86442.1, ECO:0000313|Proteomes:UP000276029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19791 {ECO:0000313|EMBL:RKS86442.1,
RC ECO:0000313|Proteomes:UP000276029};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKS86442.1}.
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DR EMBL; RBWX01000010; RKS86442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495RG16; -.
DR Proteomes; UP000276029; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 17..495
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 879..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 556..562
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 128
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 904 AA; 99387 MW; A6D7770149E7C868 CRC64;
MDAPETSGAE PSDIRPISIV EEMKTSYLDY AMSVIVARAL PDVRDGLKPV HRRILYTAYE
NGFTSNKPYR KSARIVGDVM GKYHPHGDSA IYDALVRMAQ DWSMRVPLID GQGNFGSMDP
DAAAAMRYTE SRLAKVTDEL LTDLDKDTVD FVPNYDGSES EPSVLPARFP NLLVNGAGGI
AVGMATNIPP HNLGEVVAAA VAFIDNPAIT VEELMEFVPA PDFPTGAMVM GKGGLLSAYT
TGRGSVIMRA RSIVEDRRGD RRQIVLTEIP FQVGKAGLVE KIAEAVKDKR IEGVSDIRDE
SNREGVRVVI ELKRDATPEV VLNQVYRFTP AQTSFAFNML AIRGGRPELL NLRDIIAAFI
TFREEVITRR SKFELNKARD RAHILLGLVV AVSNLDEVVR IIRGSSNPAE ARETLMAREW
AIGEIRPYLE LVEAVEGAVY GDSYKMSEIQ VRAILDLRLH RLTQLGREEI GGELKELAVS
IAELLAILGD RAKLYAVMRE ELVAVSEGYA TPRRTEIVPY LDDIDDEDLI EREEMVVTVT
MGGYIKRTPL DSFRAQRRGG KGRSGMNTKD EDAITNLFVT LTHTPVLFFS TAGKVYRMKV
WKLPEGAPQA RGRAMANLLP LADGEVISTV LPLPEDEAEW GKLHVMFATA KGTVRRNSMD
AFTNVPSNGK IAMRFDEDSD DRLIGVALLT EDDDVLLATR QGKAIRFSAT DVREFQSRTS
TGVRGMTLKG DDEVISLSIL RGFAATPDER EAYLRAAPWK DNENEPTLSP ERMAEFTAAE
EFILTVCANG YGKRTSAYEY RRTNRGGQGI GNIDNIARNG PVVASFPAHD GEQLMLVTDQ
AKMIRLGLDT LRVIGRNSAG VRLFNVADNE HVVSAAKIAT DGEDEGEDEG ADAAEEVEAA
PATE
//
