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Database: UniProt
Entry: A0A0M8KRH0_9MICO
LinkDB: A0A0M8KRH0_9MICO
Original site: A0A0M8KRH0_9MICO 
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
//
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