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Database: UniProt
Entry: A7BN32_9GAMM
LinkDB: A7BN32_9GAMM
Original site: A7BN32_9GAMM 
ID   A7BN32_9GAMM            Unreviewed;       248 AA.
AC   A7BN32;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=BGS_0947 {ECO:0000313|EMBL:EDN72051.1};
OS   Beggiatoa sp. SS.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=422288 {ECO:0000313|EMBL:EDN72051.1, ECO:0000313|Proteomes:UP000003533};
RN   [1] {ECO:0000313|EMBL:EDN72051.1, ECO:0000313|Proteomes:UP000003533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS {ECO:0000313|EMBL:EDN72051.1};
RA   Mussmann M., Hu F.Z., Richter M., de Beer D., Preisler A., Jorgensen B.B.,
RA   Huntemann M., Glockner F.O., Amann R., Koopman W.J.H., Janto B., Hogg J.,
RA   Boissy R., Lasken R.S., Stoodley P., Ehrlich G.D.;
RL   Submitted (MAY-2007) 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}.
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:EDN72051.1}.
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DR   EMBL; ABBY01000547; EDN72051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7BN32; -.
DR   BioCyc; BSP422288:G10LO-952-MONOMER; -.
DR   Proteomes; UP000003533; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 3.30.565.10; 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; IPR013506; Topo_IIA_bsu_dom2.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EDN72051.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003533};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          126..235
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
SQ   SEQUENCE   248 AA;  27790 MW;  4BE71F8B827B8FA3 CRC64;
     MTVLHAGGKF DTNSYKVSGG LHGVGVSVVN ALSEELHLTI YRDGKIHEQT YRDSVPVAPL
     VVTGDSDKTG SEIRFKPSAK TFTNTEYHYD ILANRLRELS FLNAGVRIRL IDERTAKDTV
     FEDEGGIRSF VELLNRNKTV LHDSVFYLLS QKDDISVEVA MQWNDSYHEN FFCFTNNIPQ
     RDGGTHLAGF RGAMTRTFNN YLEREGFLKK AKVSTSGDDV REGLTAVLSV KNARSKIFIT
     NQTQTGVK
//
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