ID Q4A1Y0_HELBI Unreviewed; 366 AA.
AC Q4A1Y0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:CAI94325.1};
OS Helicobacter bizzozeronii.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=56877 {ECO:0000313|EMBL:CAI94325.1};
RN [1] {ECO:0000313|EMBL:CAI94325.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yrjola {ECO:0000313|EMBL:CAI94325.1};
RA Laatu M.E.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAI94325.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yrjola {ECO:0000313|EMBL:CAI94325.1};
RX PubMed=17329766; DOI=10.1099/ijs.0.64462-0;
RA Hannula M., Hanninen M.L.;
RT "Phylogenetic analysis of Helicobacter species based on partial gyrB gene
RT sequences.";
RL Int. J. Syst. Evol. Microbiol. 57:444-449(2007).
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AJ969189; CAI94325.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4A1Y0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 302..366
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAI94325.1"
FT NON_TER 366
FT /evidence="ECO:0000313|EMBL:CAI94325.1"
SQ SEQUENCE 366 AA; 40287 MW; 69DF5A37F406D20D CRC64;
GLHGVGVSVV NALSTKLIMT IKRGGQIFRQ EFAKGIPTTP LEVVGTTKEQ GTSIEFFPDP
SIMEVVAFDS SVLQKRFQEM AYLNHGLTIH FEDQPHQIKE TYHYAAGLKQ FILDNNKNPL
ISEVIAFSAQ AEDMEVEIAL AYNEGYSEQM FSFVNSIRTP EGGTHESGFR MGLSRAILNY
IQENANAREK EAGVVQEDIK EGLLAVVSAR ILEPQFEGQT KAKLGSSFVR PVVAKLVYEK
MAKFFEENPS VARAIMQKAL LAAKGREAAK KAKELTRKKD NLSVGTLPGK LADCQSKDPK
ECEIYLVEGD SAGGSAKQGR DRVFQAILPL RGKILNVEKS HLGKILKSEE IKNMITAFGC
GVGQEF
//
