ID A0A0M8KRH0_9MICO Unreviewed; 954 AA.
AC A0A0M8KRH0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=Y09_3326 {ECO:0000313|EMBL:GAP80467.1};
OS Brachybacterium sp. SW0106-09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1704590 {ECO:0000313|EMBL:GAP80467.1, ECO:0000313|Proteomes:UP000037781};
RN [1] {ECO:0000313|EMBL:GAP80467.1, ECO:0000313|Proteomes:UP000037781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW0106-09 {ECO:0000313|EMBL:GAP80467.1,
RC ECO:0000313|Proteomes:UP000037781};
RA Qin Q.L., Li Y., Zhang Y.Z.;
RT "Genome Sequencing of Brachybacterium sp. SW0106-09.";
RL Submitted (SEP-2015) 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 topoisomerase GyrA/ParC subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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:GAP80467.1}.
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DR EMBL; BCAK01000060; GAP80467.1; -; Genomic_DNA.
DR RefSeq; WP_053918936.1; NZ_BCAK01000060.1.
DR AlphaFoldDB; A0A0M8KRH0; -.
DR Proteomes; UP000037781; 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 68..525
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 586..592
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 954 AA; 104288 MW; 2C7CD1075915061F CRC64;
MSDTPNDPTG PEDDQSSAET PTPAESAGIG GQEMPEGSSE LSADEAASRT VTLVDPLDED
EVDRITQVDL NQEMQRSYLD YAMSVIVSRA LPDVRDGLKP VHRRIVYAMY DGGYRPDRSF
SKCAKVVGEV MGNYHPHGDS AIYDAMVRLV QPWNMRYPLI LGQGNFGSAG DDGAAAPRYT
ECKMAPLALE LVRDIEQDTV DMQGNYDNTV DEPSVLPARF PNLLVNGSAG IAVGMATNIP
PHNLREVAGA VQWLLTNHEA TKPELLEACL RFIKGPDFPS GATIVGTDGI EDAYRTGRGS
ITQRAVVSTE EINGRMALVV TELPYQVNPD NLARKIAEMV KLGKIQGIAD ITDETSGRTG
QRLVITLKRD AVAKVVLNNL YKHTQLQENF SANMLALSGG VPRTLSIDSF VREWTKHQID
VIVRRTKFRL RKAEEQIHIY RGYLKALDAL DEVIALIRRS PDVDEARTGL IDLLEIDEIQ
ANAILAMQLR RLAALERQKI IEEHDRLQAL IEEYTAILAD PARQRQIVSE ELGELVDKYG
DDRRTQILPF HGDMSMEDLI PEEDVVVTIT RGGYVKRTRE DQYRAQKRGG KGVRGASLRE
DDVVEHFFTT TTHRWLLFFT NQGRVYRAKG YELPEAPRDA KGQHVANLMA FQPDEHIASV
LAIDSYEDAE YLVLATESGL VKKTAMTAFD SNRTGGIIAI NLRDIDGIDG TRPDRVIAAR
AVNGDDELLL VSRNGQSVRM PAADDVLRPT GRATSGVTGM KFRHDDQLLA MDVVRPGTFV
VTVTDGGFAK RTSVDEYRLQ GRGGLGIRVA KLPDDRGHLA GAAVVEETDE LLVVMERGRV
VRSKVSEVPP KGRTTMGVTF AKPDKGDRIL LVTTGPESEL DEDEAEKPVL EDAGDGGAES
ADSAASPASA DEAGGEEDVE ISDTAASATE GGQGDALGSD ESETSTDDAD QNEE
//