ID A0A076NDQ8_9CORY Unreviewed; 854 AA.
AC A0A076NDQ8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:SNV52673.1};
GN ORFNames=CIMIT_00060 {ECO:0000313|EMBL:AIJ32534.1}, SAMEA4535761_00078
GN {ECO:0000313|EMBL:SNV52673.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ32534.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ32534.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ32534.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SNV52673.1, ECO:0000313|Proteomes:UP000215374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13015 {ECO:0000313|EMBL:SNV52673.1,
RC ECO:0000313|Proteomes:UP000215374};
RG Pathogen Informatics;
RL Submitted (JUN-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}.
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DR EMBL; CP009211; AIJ32534.1; -; Genomic_DNA.
DR EMBL; LT906467; SNV52673.1; -; Genomic_DNA.
DR RefSeq; WP_038587439.1; NZ_LT906467.1.
DR AlphaFoldDB; A0A076NDQ8; -.
DR STRING; 156978.CIMIT_00060; -.
DR KEGG; cii:CIMIT_00060; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_11; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000028780; Chromosome.
DR Proteomes; UP000215374; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028780};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 17..474
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 821..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 535..541
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 823..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 854 AA; 94785 MW; 061001E382584D18 CRC64;
MSDDTLGGGG FDAIQPIDIN EEMQTSYIDY AMSVIVGRAL PEVRDGMKPV HRRVIYAMYD
AGFRPERSFV KSVKAVGETM SNYHPHGDSA IYDTLVRMAQ PWAMRYPLVD GQGNFGSPGN
DGPAAMRYTE CKLTPLAMEM VRDIRENAVD FSPNFDSKTR EPDVLPSRVP NLLMNGSNGI
AVGMATNIPP HNLNELAEAI YWILDNHDAD EKTTLDAVLK YVKGPDFPTA GLVVGDKGIK
EAYTTGRGSI RMRGVTEIEE VGNRQVIVIT ELPYQVNPDN FIHNIADQVN AGKMAGIADI
DDESSDRIGM RIVVRLKRDA VPRVVLNNLY KHSQLETNFS ANMLSIVDGV PRTLRLDQML
RYYVQHQIEV IVRRTQYRLD EAEKRAHILR GLVKALDALD EVIALIRRSP TVDDARQGLM
KLLDVDEIQA NEILAMQLRR LAALERQKIV DDLAEIERQI ADYKDILAKP ERQREIVATE
LKEIVDKFGD ERRTQIVAAT GDVTEEDLIA RENVVVTITS TGYAKRTKVD AYKSQKRGGK
GVRGAELKQD DVVKHFFICS THDWILFFTN FGRVYRLKAY ELPEAGRTAR GQHVANLLEF
QPEEKIAQII QIQSYEDAPY LVLATRDGRV KKSRLTDYES ARSAGLIAIN LNEGDALIGA
ALTNEEDDIL LVSEQGQAIR FAADDDQLRP MGRATAGVKG MRFRDDDQLL AMTVVQDGEY
LLVATSGGYG KRTAIEEYNQ QGRGGMGVMT FKYTPKRGKL IGALAVDEED QIFAITSAGG
VIRTEVNQIR PSSRATMGVR LVDLADDVEL LAIDVNVEDS GEEEATAVAK GEKTLEEAQE
ATQSSISGGP EGEE
//
