ID A0A2V5LL59_9MICC Unreviewed; 897 AA.
AC A0A2V5LL59;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=CVV68_07050 {ECO:0000313|EMBL:PYI68090.1};
OS Arthrobacter livingstonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI68090.1, ECO:0000313|Proteomes:UP000247832};
RN [1] {ECO:0000313|EMBL:PYI68090.1, ECO:0000313|Proteomes:UP000247832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LI2 {ECO:0000313|EMBL:PYI68090.1,
RC ECO:0000313|Proteomes:UP000247832};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-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:PYI68090.1}.
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DR EMBL; QJVD01000006; PYI68090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5LL59; -.
DR SMR; A0A2V5LL59; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000247832; 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 34..491
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 833..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 553..559
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 145
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 897 AA; 99412 MW; BB537187C8093342 CRC64;
MSDETPENPG SENIDGSGEV VLTGDVLHDK VEQIDLQEEM KRSYLDYAMA VIVGRALPDV
RDGLKPVHRR VLYAMFDGGY RPDRSFNKCA RVVGEVMGQY HPHGDSSIYD ALVRLIQDWT
MRYPLALGQG NFGSPGNDGA AAPRYTETKM APLAMEMVRD IDEETVDFQD NYDGKNQEPT
ILPARYPNLL VNGSSGIAVG MATNIPPHNL REVSAGVQWY LANPTVSREE LLEALIERIK
GPDFPTGAQI LGRKGIEDAY RTGRGSITMR AVVNVEEIQG RTCLVVTELP YQANPDNLAI
KIAELVKDGK ISGIADLRDE TSGRTGQRLV VVLKRDAVAK VVLNNLYKHT QLQENFGANM
LAIVDGVPRT LPLDAFIRHW VTHQMDVIVR RTRFRLRKAE EEAHIQRALL KALNALDEVI
ALIRRSSTSE EARDGLMALL DIDEIQAKAI LDMQLRKLAA LEHQKIQDRS DVLETMITEF
NRILADPEVQ RGIVSDELAD ITARYGDDRR TEIMMGYDPN MSMEDLIPEE EMVVTITRGG
YVKRTRSDNY RTQHRGGKGI KGAQLRGDDV VEHFFVTTTH HWLLFFTNLG RVYRAKAYEL
AEAGRDAKGQ HVANLMAFQP DEKIAQVMEL KDYQQSPYLV LATRNGLVKK TRLEDYDTNR
SAGVIAINLR DDDELVSAQL VSDTDDLLLV SRKGQSIRFT ATNEALRPMG RATSGVTGMK
FRERDELLAA NVVTDDSFVF IVTEGGYAKR TAVSEYRLQG RGGLGIKVAK LVEDRGDLVG
ALIVREDDEV LVVMSGGKIV RSDVAEVPAK GRDTMGVIFA KPDKNDRIIE VARNSERGLD
NDDDAENGEI PADEGGTDGD TGVEPAADTV DNDAFEANVQ PDEVPLNDHD ATNGGTD
//
