ID A0A2P1PU07_9GAMM Unreviewed; 878 AA.
AC A0A2P1PU07;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=C7S18_14505 {ECO:0000313|EMBL:AVP98327.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP98327.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP98327.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP98327.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP98327.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP98327.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-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}.
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DR EMBL; CP027860; AVP98327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1PU07; -.
DR KEGG; xba:C7S18_14505; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000241074; 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:UP000241074};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..499
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 845..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 560..566
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 878 AA; 97089 MW; F9A3B3DE73722CC1 CRC64;
MSEFAKEVIK VNIEDEMRQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNELGSHYN
KPYYKSARIV GDVIGKYHPH GDSSVYDTLV RMAQPFSLRS ILVDGQGNFG SVDGDPAAAM
RYTEARLSKL AHELMADIDK ETVDFTPNYD EKELEPTVLP TRFPNLLVNG SAGIAVGMAT
NIPPHNLGEV IDGAIALIDA PELGIDDLMQ YIPGPDFPTG GTINGASGII DAYRTGRGRI
LIRAKCEIET DDDGRDAIIV TELPYQVNKA RLIEKIAELV KEKKVEGIAP DLRDESDKDG
MRIYIPIKRN ESAEVVLNNL LAQTQLEVVF GINIVALVDG QPKTLNLKEM LDAFIRHRRE
VVTRRTIFDL RKARERAHVL EGLTVALANI DEMIELIKTS PNAQVARERL LARVWEPGLV
RALLGERGAS QSRPESLSDH EGLLEHGYQL SEVQVKEILD MRLNKLTGLE QEKLTDEYKV
LLETIRGLIE ILEDPIKLLA VIRDELVNVK EEFADPRRTI IQVNQDDLRN EDLIDKQDLV
VTMSHAGYVK AQPVTDYRAQ RRGGKGRSAT AMKNEDFIEN ILVAHSHDTV LCFTSSGRVF
WLRTFEFPMA GPGARGRPIV NLLPSLEAGE KINAMLPVRE YRHDHYVFFA TQAGVVKKTP
LSEFSRRRSS GIRAVELDDG DRLIDVAITD GSRDVMLFAS NGKAVRFAED EVRAVGRTAR
GVRGMTLALG ERVVSMIVAD LGDILTATER GFGKRTELEE FPKKGRGTQG VIAIQTSERN
GNLVGAVQVT EVHEVMLISN QGTLVRTRVS EIAQVGRNTQ GVTLIRLPDD EALVSFAKVE
ALPEDLSEAA ELEAPPAPPA DADHAAEGQT PPAGTESE
//
