ID A1L093_9GAMM Unreviewed; 372 AA.
AC A1L093;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:AAY46859.1};
OS Aeromonas sp. RK 70363.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=329131 {ECO:0000313|EMBL:AAY46859.1};
RN [1] {ECO:0000313|EMBL:AAY46859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RK 70363 {ECO:0000313|EMBL:AAY46859.1};
RA Jangid K., Gonzalez J.M., Whitman W.B., Kong R., Patole M.S., Shouche Y.S.;
RT "A multigene approach to Aeromonas taxonomy.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AY987531; AAY46859.1; -; Genomic_DNA.
DR AlphaFoldDB; A1L093; -.
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 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 303..372
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY46859.1"
FT NON_TER 372
FT /evidence="ECO:0000313|EMBL:AAY46859.1"
SQ SEQUENCE 372 AA; 41041 MW; 0504A3E612635060 CRC64;
HGVAPSVVNA LSDKLLLTIR RNGHVYEQTY HLGEPQAPLK QIGDSSSGTG TEVRFWPSPT
IFTDTLYHYE ILAKRLRELS FLNSGVSIRL QDERDGREVH FCYEGGIKAF VEYLNQNKTP
IHPKVFHFST EQDGIGVEVA MQWNDAYQEG VYCFTNNIPQ RDGGTHLVGF RTALTRTLNT
YMDKEDYSKK AKSAASGDDV REGLIAVISV KVPDPKFSSQ TKDKLVSSEV KTAVEQAMGE
KLGEFLLENP GDAKIVVNKI IDAARAREAA RKARELTRRK GALDIAGLPG KLADCQEKDP
ALSELYIVEG DSAGGSAKQG RNRKNQAILP LKGKILNVEK ARFDKMISSQ EVGTLITALG
CGIGRDEYNP DK
//