ID A0A2M9CCW7_9CELL Unreviewed; 868 AA.
AC A0A2M9CCW7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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=CLV28_2610 {ECO:0000313|EMBL:PJJ69153.1};
OS Sediminihabitans luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Sediminihabitans.
OX NCBI_TaxID=1138585 {ECO:0000313|EMBL:PJJ69153.1, ECO:0000313|Proteomes:UP000231693};
RN [1] {ECO:0000313|EMBL:PJJ69153.1, ECO:0000313|Proteomes:UP000231693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25478 {ECO:0000313|EMBL:PJJ69153.1,
RC ECO:0000313|Proteomes:UP000231693};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ69153.1}.
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DR EMBL; PGFE01000005; PJJ69153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9CCW7; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000231693; 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:UP000231693};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 37..494
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 849..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 459..493
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 555..561
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 148
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 868 AA; 96511 MW; CD20E9EC930B4F63 CRC64;
MTDETPEQDQ TGGVPTGEEA VAAAAALAVQ HGRIEQVDLQ LEMQRSYLDY AMSVIVGRAL
PDVRDGLKPV HRRVVYAMYD GGYRPDRAYS KCSRVVGDVM GKFHPHGDSA IYDALVRLVQ
DWSLRYPLVA GQGNFGSPGN DPAAAPRYTE CRMAPLAMEM VRDIDKDTVD FQDNYDGRTQ
EPAILPSRFP NLLVNGSAGI AVGMATNIPP HNLREVADGV RWHLAHPEAS REELLEQLLK
LVKGPDFPTG ATILGHKGIE EAYRTGRGSI TMRAVVNVEE IQNRICLVIT ELPYQVNPDN
LALKIADLVK DGRMQGIADI RDETSGRTGQ RLVIVLKRDA VAKVVLNNLY KHTQLQDNFS
ANMLALVDGV PRTLSIDAFV RHWTTHQIEV VVRRTRYLLN DAEQRIHIYR GYLKALDQLD
EVIALIRRSP DADQARVGLM ELLDVDERQA RAILDMQLRR LAALQRQEII DEHDKLEREI
TEYQAILASE QRQRDIVGAE MDEIVDKYGD ERRTTILPYD GEVSMEDLIA EEEVVVTITR
GGYVKRTRSD NYRAQKRGGK GVRGAQLRED DIVDQFFVTT THHWLLFFTN LGRVYRAKAY
ELPEGGRDAK GQHVANLLAF QPGETIAQVM ELRDYDAAEY LVLATRRGLV KKTRLSEYNS
PRTGGLIAIN LREDDEGVTD ELVSARLVNA DDHLILVSRK GQSIRFEAND DAMRPLGRAT
SGVTGMKFRD GDELLSADVV EDGSDLFVVT EGGFAKRTRI SEYRVQGRGG LGIKVANLVE
ARGDLVGALI TEADDEVLVI MERGKIVRSA VSEVNLTGRT TQGVTFAKPG KGDRIIAVAR
NVERRLEGDG DTVIEDGAHD APATSEEV
//
