ID A0A3A5MBU9_9MICC Unreviewed; 891 AA.
AC A0A3A5MBU9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:RJT80192.1};
GN ORFNames=D6T63_10055 {ECO:0000313|EMBL:RJT80192.1};
OS Arthrobacter cheniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1258888 {ECO:0000313|EMBL:RJT80192.1, ECO:0000313|Proteomes:UP000272560};
RN [1] {ECO:0000313|EMBL:RJT80192.1, ECO:0000313|Proteomes:UP000272560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hz2 {ECO:0000313|EMBL:RJT80192.1,
RC ECO:0000313|Proteomes:UP000272560};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Arthrobacter.";
RL Submitted (SEP-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:RJT80192.1}.
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DR EMBL; QZVT01000004; RJT80192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5MBU9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000272560; 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 28..485
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 856..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..553
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 864..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 891 AA; 98614 MW; FBED01D28EDBD2BA CRC64;
MSDVTTGNGN GPDEPLEGEV LTDRVEQVDL QTEMQRSYLD YAMAVIVGRA LPDVRDGLKP
VHRRVLYAMF DGGYRPDRSF NKCARVVGEV MGQYHPHGDS AIYDALVRLI QDWTMRYPLA
LGQGNFGSPG NDGAAAPRYT ETKMAPLAME MVRDIDEETV DFQDNYDGKN QEPTILPSRF
PNLLVNGSSG IAVGMATNIP PHNLREVADG VQWYLENPEA SKEELLEALI TRIKGPDFPT
GAQILGHKGI EDAYRTGRGS ITMRAVVNVE EIQNRTCLVV TELPYQANPD NLAIKIAELV
KDGKVSGIAD LRDETSGRTG QRLVIVLKRD AVAKVVLNNL YKHTQLQDNF SANMLAIVDD
VPRTLSLDAF VRHWVTHQLE VIVRRTRYRL RKAEEEAHIL RGLLKALDAL DEVIALIRAS
STTEEARDGL MGLLSIDELQ ATAILNMQLR RLAALERQKI QDRHAELETM ITEFNRILAS
EDVQRGIVST ELSDIVAKFG DDRRTEILMG YDGDMSMEDL IPEEEMVVTI TRGGYVKRTR
SDNYRQQARG GKGIKGAQLR GDDVVEHFFV TTTHHWLLFF TNLGRVYRAK AYELVEAARD
AKGQHVANLL AFQPDETIAQ VLDLRDYQQS PYLVLATKRG LVKKTRLEDY DTNRTAGVIA
INLRDNDELV SAQLVSGSDD IMLVSRKGQS LRFTADDDAL RPMGRATSGV TGMKFREDDE
LLAANVVTDD SFVFIVTEGG FAKRTRVDDY RVQGRGGLGI KVAKLAEERG DLIGALVVQE
EDEVLVVMGG GKVVRSAVTG VPAKGRDTMG VIFAKPDKTD RIIAIARNSE RSVGVEEGLI
EDPSEASPDV EVIDTVTPAE EPAEFTADEV RLSTEETAEP DAESPEHGGN E
//
