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Database: UniProt
Entry: A1L0A4_9GAMM
LinkDB: A1L0A4_9GAMM
Original site: A1L0A4_9GAMM 
ID   A1L0A4_9GAMM            Unreviewed;       371 AA.
AC   A1L0A4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:AAY46870.1};
OS   Aeromonas sp. SF8-170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=329132 {ECO:0000313|EMBL:AAY46870.1};
RN   [1] {ECO:0000313|EMBL:AAY46870.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SF8-170 {ECO:0000313|EMBL:AAY46870.1};
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; AY987542; AAY46870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1L0A4; -.
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          302..371
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY46870.1"
FT   NON_TER         371
FT                   /evidence="ECO:0000313|EMBL:AAY46870.1"
SQ   SEQUENCE   371 AA;  41067 MW;  541403ED890B2A09 CRC64;
     HGVGVSVVNA LSEKLLLTIR RNGHVYEQTY HMGEPQAPLK QIGDSNGTGT EVRFWPSATI
     FTDTLYHYEI LAKRLRELSF LNSGVSIRLQ DERDGREVHF CYEGGIKAFV EYLNQNKTPI
     HPKVFHFSTE QDGIGVKVAM QWNDAYQEGV YCFTNNIPQR DGGTHLVGFR TALTRTLNTY
     MDKEDHSKKA KSAASGDDVR EGLIAVISVK VPDPKFSSQT KDKLVSSEVK TAVEQTMGEK
     LGEFLLENPG DAKIVVNKII DAARAREAAR KARELTRRNG ALDITGLLGK LADCQEKDPA
     LSELYIVEGD SAGGSAKQGR NRKNQAILPL KGKILNVERA RFDRMISSQE VGTLITALGC
     GIGRDEYNPD K
//
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