ID Q93DP2_9ALTE Unreviewed; 392 AA.
AC Q93DP2;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:AAL01491.1};
OS bacterium PV-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae.
OX NCBI_TaxID=163925 {ECO:0000313|EMBL:AAL01491.1};
RN [1] {ECO:0000313|EMBL:AAL01491.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PV-4 {ECO:0000313|EMBL:AAL01491.1};
RX PubMed=11493693; DOI=10.1073/pnas.171178898;
RA Murray A.E., Lies D., Li G., Nealson K., Zhou J., Tiedje J.M.;
RT "DNA/DNA hybridization to microarrays reveals gene-specific differences
RT between closely related microbial genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9853-9858(2001).
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; AF387352; AAL01491.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93DP2; -.
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 316..392
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAL01491.1"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:AAL01491.1"
SQ SEQUENCE 392 AA; 43405 MW; 325749640F7DEDCA CRC64;
KFDDNSYKVS GGLHGVGVSV VNALSEKLKL TIRRDGKLYE QFYTMGEPDA PIAEIGDATN
TGTEIRFWPS AETFSDTLFH FDILAKRVRE LSFLNSGVGI RLIDERDNKD EFFKYEGGIS
AFVDYLNLNK TPVNKEIFHF VQEREDGITV EVAMQWNDGF QENIFCFTNN IPQRDGGTHL
AGFRAALTRN LNSYMDKEGF NKKGKTSATG DDAREGLTAV ISVKVPDPKF SSQTKDKLVS
SEVKSAVEQT MGEKLGDYLL ENPNEAKLIV GKIIDAARAR EAARKAREMT RRKGALDLGG
LPGKLADCQE KDPALSEIYI VEGDSAGGSA KQGRNRKNQA ILPLKGKILN VEKARFDKML
SSQEVATLIT ALGCGIGRDE YDPDKTRYHN IV
//
