ID A0A2T8HX10_9RHOB Unreviewed; 933 AA.
AC A0A2T8HX10;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=DDE20_07575 {ECO:0000313|EMBL:PVH29944.1};
OS Pararhodobacter oceanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=2172121 {ECO:0000313|EMBL:PVH29944.1, ECO:0000313|Proteomes:UP000245911};
RN [1] {ECO:0000313|EMBL:PVH29944.1, ECO:0000313|Proteomes:UP000245911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM505 {ECO:0000313|EMBL:PVH29944.1,
RC ECO:0000313|Proteomes:UP000245911};
RA Wang X.-L., Du Z.-J.;
RT "Pararhodobacter oceanense sp. nov., isolated from marine intertidal
RT sediment.";
RL Submitted (APR-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:PVH29944.1}.
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DR EMBL; QDKM01000002; PVH29944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HX10; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000245911; 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:UP000245911};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 21..500
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 896..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 561..567
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 933 AA; 102811 MW; 4DFFB6E5D0772243 CRC64;
MSDDTQIPDD IDRTPPASPA ISIVEEMRTS YLDYAMSVIV SRAIPDLRDG LKPVHRRILY
AMHETNNTHD KSYRKSARPV GDVMGKFHPH GDSAIYDALV RMAQPFSMSL KLLDGQGNFG
SMDGDNPAAM RYTEVRMDKT ANYLLADIDK DTVDFQDNYD GKDREPTVLP ARFPNMLVNG
AGGIAVGMAT NIPPHNLGEV IDATKALIEN PDLTSEQLMQ FVPAPDFPTG GQIMGRGGAR
KAYLEGRGSV IIRAKTHVEE LRKDRFAIII DEIPYQVNKS QMVEKIAEAV RDKRIEGIAH
VADESDRIGV RVVVELKRDA TPDVVLNQLF RFTPMQTSFG CNMLALNGGR PEQLMLRDFL
TNFVDFREEV VTRRTAYELN KARERSHILC GLAVAVSNVD EVVATIRSSA DPADARQKLM
TRRWPASDIA AYIRLIDDPS HTLNDDGTYN LSELQARAIL ELRLQRLTAM GVREVTDELE
ELAGKIKDYL DILRSRSRIM AIINDELDEV RSLFAVPRRT EIVDWAGDMD DEDLIEREDM
VVTITSGGYI KRTPLMDFRA QNRGGKGLSS MSTKEDDVVT TLFVANTHTH LLFFTTDGMV
YKIKCWRLPL AGRNARGKAI VNILPIPNGV SIAALMPVDA PEEEWENLQI VFATSQGDVR
RNALSDFTNV MRNGKIAMKL PEDVELVNAR IAEAEDDVML LTAMGRAIRF SSTDVRVFKG
RDSTGVRGIR LGDGDSVVSM AVIRHFTADP QERAAYLKQR RLMAGAADEV ESDEDDDGIE
AGQLSPERYA EMSAAEDLIL TVTERGAGKL SSSHDYPVRG RGGQGVMAMD RAMRGGPLIA
AFPVVNGDQI MLATSTGQSI RVPVDQISFR SRSAGGVRVF NTGKDEVVVS VARVAESEAE
PDAEVPADAI TEIDAPATPI EGSETPPGDN SDA
//
