ID A0A1C2FXJ0_9GAMM Unreviewed; 868 AA.
AC A0A1C2FXJ0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=A9R16_04685 {ECO:0000313|EMBL:OCX43982.1}, C4900_04240
GN {ECO:0000313|EMBL:RCN58968.1};
OS Acidiferrobacter thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Acidiferrobacter.
OX NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX43982.1};
RN [1] {ECO:0000313|EMBL:OCX43982.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ {ECO:0000313|EMBL:OCX43982.1};
RA Ma L.;
RT "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a Distinctive
RT Species of Ectothiorhodospiraceae.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RCN58968.1, ECO:0000313|Proteomes:UP000253250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M-1 {ECO:0000313|EMBL:RCN58968.1}, and m-1
RC {ECO:0000313|Proteomes:UP000253250};
RA Issotta F., Thyssen C., Mena C., Moya A., Bellenberg S., Sproer C.,
RA Covarrubias P.C., Sand W., Quatrini R., Vera M.;
RT "Insights into the biology of acidophilic members of the
RT Acidiferrobacteraceae family derived from comparative genomic analyses.";
RL Submitted (FEB-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:OCX43982.1}.
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DR EMBL; MDCF01000239; OCX43982.1; -; Genomic_DNA.
DR EMBL; PSYR01000001; RCN58968.1; -; Genomic_DNA.
DR RefSeq; WP_065972168.1; NZ_PSYR01000001.1.
DR STRING; 163359.A9R16_04685; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000253250; 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 11..498
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 847..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..565
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 868 AA; 95342 MW; C5DD997574E03E9C CRC64;
MDQFAKETIP VNLEEEMRQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMRELGNDWN
RPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQTFSMRY PLVDGQGNFG SVDGDAPAAM
RYTEIRMARV AHELLADLDK ETVDFTPNYD GSEHEPSVLP TAIPNLLVNG SSGIAVGMAT
NIPPHNLSEV INALLALIEN PDLSVEALMA YIPGPDFPTA AIINGNAGIR EAYVTGRGKI
YVRSRVEIEE ERPGHRQALI VNELPYQVNK ARLLEKIAEL VKEGRLEGIA ELRDESDKSG
MRMVIELKRG ENAEVILNNL YQQTALQTVF GINMVALEDG QPRLLSLPQI LKAFLSHRRE
VVTRRTLYEL RKSRERAHIL EGLAVALENI DAIIALIKAA PDPATARQAL LGRPWSARFV
ADLLRHAGPH SRLEGLPADV GLREDRYVLT DTQAQAILDL RLHRLTGLEQ DKIHEEYQEI
LRKIEGLSEI LRSEARLMAV IAEELAAIKA QYGDERRTEI LAGRLDLSRE DLIAQETVVV
TLSHAGYAKC QPLADYRAQR RGGKGRSFGR MREQDFVDRL VVANTHDTVL CFSNRGKAYW
LKVYDLPQTG HGAQGRPIVN FLPLAEGEKL TAILPLAAFE EGKSVFMATS DGTVKKTPLA
DFSRPRTSGI VAIDLVDGNV LVGAGIANGN SDILLFSDAG KAVRFQESDV RSMGRNARGV
RGLSLRKGQR LVSLMIADPA AGDQVVLVAS ANGYGKRTPF SEFPRHNRGG QGVISMQVTE
RNGAIVGAVL AGDDDEVMMI TDTGSLIRMC AREISLQSRN TQGVRLMGLD ANERLVSVEK
IEETAALGGE VGTETQAMDA GDDDGADL
//
