ID A0A1H6KTP9_9FLAO Unreviewed; 861 AA.
AC A0A1H6KTP9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN02927937_01326 {ECO:0000313|EMBL:SEH76953.1};
OS Paenimyroides aquimaris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEH76953.1, ECO:0000313|Proteomes:UP000199634};
RN [1] {ECO:0000313|EMBL:SEH76953.1, ECO:0000313|Proteomes:UP000199634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEH76953.1,
RC ECO:0000313|Proteomes:UP000199634};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNXE01000015; SEH76953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6KTP9; -.
DR STRING; 1159016.SAMN02927937_01326; -.
DR Proteomes; UP000199634; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000199634};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..463
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 840..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..476
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 524..530
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 861 AA; 97282 MW; DDACA8BDAE6B974C CRC64;
MISDGEKLIP INIEEEMKSA YIDYSMSVIV SRALPDVRDG LKPVHRRVLF GMYELGVTAS
KAHKKSARIV GEVLGKYHPH GDKSVYDAMV RMAQEWSLRY LLVDGQGNFG SVDGDDPAAM
RYTEARMKKL AEEILADIDK ETVDFQLNFD DTLEEPKVMP TKIPTLLVNG ASGIAVGMAT
NMAPHNLTEV INGTLAYIDN NDIEIDELMQ HIKAPDFPTG GIIYGYEGVK EAYKTGRGRV
VMRAKANFEE VDGKECIVVT EIPYQVNKAE MIKKTAELVN DKKIEGISTI RDESDRKGMR
IVYVLKREAV PNIVLNMLYK FTQLQSSFSI NNIALVNGRP QLLNLKELIH YFVEHRHDVV
TRRAEYELRK AQERAHILEG LIIASDNIDE VIAIIRSSKN ADEARERLIE RFSLSEIQAR
AIVEMRLRQL TGLEQEKLRA EFDEIMKLIA RLQELLASKE MRMNLIKEEL TEIRDKYGDD
RRSDIEYAGG EMNIEDLIAD EQVVITISHA GYIKRTPLSE YKTQNRGGVG QKSAGTRDQD
FLEHMYVATN HQYMLFFTQK GKCFWLRVYE IPEGTKQAKG RAIQNLINIE NDDKVKAFIC
TQDLRDEEYI NNHYIVMCTK QGQVKKTALE QYSRPRQNGI NAITIKEGDE LLEAKLTDGN
SKVLVAAKNG KMVRFDESKT RPMGRTASGV RGIKLAGEND EVIGLVTVSD LNSEILVVSE
NGYGKRSSLE AYRETNRGGK GVKAMNITDK TGALISINSV TDNDDLMIIN KSGLTIRLRV
SDLRVMGRNT QGVRLINIKG NDSIAAVAKV MRDEDEENEM DDELKKDLLA VDENDIIEDV
VDEIEEEDDD LEEDSEETNE E
//