ID Q7CZ37_AGRFC Unreviewed; 906 AA.
AC Q7CZ37;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 132.
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:AAK87298.2};
GN OrderedLocusNames=Atu1507 {ECO:0000313|EMBL:AAK87298.2};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK87298.2, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK87298.2, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK87298.2, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK87298.2; -; Genomic_DNA.
DR RefSeq; NP_354513.2; NC_003062.2.
DR AlphaFoldDB; Q7CZ37; -.
DR STRING; 176299.Atu1507; -.
DR EnsemblBacteria; AAK87298; AAK87298; Atu1507.
DR KEGG; atu:Atu1507; -.
DR PATRIC; fig|176299.10.peg.1534; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OrthoDB; 9806486at2; -.
DR PhylomeDB; Q7CZ37; -.
DR BioCyc; AGRO:ATU1507-MONOMER; -.
DR Proteomes; UP000000813; Chromosome circular.
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:UP000000813};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 1..474
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 870..906
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 877..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 906 AA; 100834 MW; 362435F92569AFDD CRC64;
MQRSYLDYAM SVIVSRALPD VRDGLKPVHR RILYGMSELG IDWNKKYVKC ARVTGDVMGK
FHPHGNSAIY DALARMAQDW SLRLPLIDGQ GNFGSIDGDP PAAERYTECR LEKAAHSLLD
DLDKETVDFR DNYDGTLQEP VVVPAKFPNL LVNGAGGIAV GMATNIPPHN LSEVIDGCVA
LIENPAIELP EMMQIIPGPD FPTGALIMGR SGIRSAYETG RGSVIMRGVA TIEPMRGDRE
QIIITEVPYQ VNKASMIEKM AELVKEKRIE GISDLRDESD RQGYRVVIEL KRDANAEVIL
NQLYRYTPLQ TSFGCNMVAL NGGKPEQMTL LDMLRAFVSF REDVVSRRTK YLLRKARDRA
HVLVGLAISV ANIDEVIRVI RHAPDPASAR EQLMTRRWPA QDVESLIRLI DDPRHRINED
GTYNLSEEQA RAILELRLAR LTALGRDEIG DELNKIGAEI SEYLDILSSR VRIQQIVKDE
LVSIRDEFGT PRRSQIVEGG PDMDDEDLIA REDMVVTVSH LGYIKRVPLT TYRAQRRGGK
GRSGMATRDE DFVNRLFVAN THTPVLFFSS RGIVYKEKVW RLPIGTPQSK GKALINMLPL
EPGERITTIM PLPEDETAWE TLDVMFSTTR GTVRRNKLGD FVQVNRNGKI AMKLDEEGDE
ILSVETCTDR DDVLLTTALG QCIRFPVDDV RVFAGRNSVG VRGINMAEGD RIISMTIVGH
VEAEPWERAA YLKRSATERR AAGVDEEDIA LVGEEVTEEG ELSEERYQEL KAREEFVLTV
SVKGFGKRSS SYDFRTSGRG GKGIRATDTA KTNEIGELVA AFPVEEGDQI MLVSDGGQLI
RVPVNGIRIA SRATKGVTIF STAKDEKVVS VERINEPEGD DEAENGNDDE ADDNLPDAPE
APESEA
//
