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Entry: I1Z7J9_9GAMM
LinkDB: I1Z7J9_9GAMM
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ID   I1Z7J9_9GAMM            Unreviewed;       284 AA.
AC   I1Z7J9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
OS   Acinetobacter tjernbergiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=202955 {ECO:0000313|EMBL:AFJ15259.1};
RN   [1] {ECO:0000313|EMBL:AFJ15259.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 50768 {ECO:0000313|EMBL:AFJ15259.1};
RA   Narciso da Rocha C., Vaz-Moreira I., Svensson-Stadler L., Moore E.R.B.,
RA   Manaia C.M.;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFJ15259.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 50768 {ECO:0000313|EMBL:AFJ15259.1};
RX   PubMed=22669636; DOI=10.1007/s00253-012-4190-1;
RA   Narciso-da-Rocha C., Vaz-Moreira I., Svensson-Stadler L., Moore E.R.,
RA   Manaia C.M.;
RT   "Diversity and antibiotic resistance of Acinetobacter spp. in water from
RT   the source to the tap.";
RL   Appl. Microbiol. Biotechnol. 97:329-340(2013).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       modulate DNA topology and maintain chromosomes in an underwound state.
CC       Negative supercoiling favors strand separation, and DNA replication,
CC       transcription, recombination and repair, all of which involve strand
CC       separation. Also able to catalyze the interconversion of other
CC       topological isomers of dsDNA rings, including catenanes and knotted
CC       rings. Type II topoisomerases break and join 2 DNA strands
CC       simultaneously in an ATP-dependent manner.
CC       {ECO:0000256|ARBA:ARBA00001978}.
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   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC       the heterotetramer, GyrA contains the active site tyrosine that forms a
CC       transient covalent intermediate with DNA, while GyrB binds cofactors
CC       and catalyzes ATP hydrolysis. {ECO:0000256|ARBA:ARBA00011234}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; JN903893; AFJ15259.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1Z7J9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.30.565.10; 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; IPR000565; Topo_IIA_B.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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          96..265
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFJ15259.1"
FT   NON_TER         284
FT                   /evidence="ECO:0000313|EMBL:AFJ15259.1"
SQ   SEQUENCE   284 AA;  31803 MW;  2C628E49A631DB48 CRC64;
     ALSKKLQLTI YRAGQMHEQE YQHGDPQYPL KVVGETDRTG TVVRFWPSEL TFSQTIFNVD
     ILARRLRELS FLNAGVKIVL RDERINFEHI YAYEGGLSEF VKYINEGKTH LNDIFHFTAD
     TDSGIAVEVA LQWNESYQEN VRCFTNNIPQ KDGGTHLAGF RAALTRGLNQ YLESENILKK
     EKVAVTGDDA REGLTAIISV KVPDPKFSSQ TKEKLVSSEV KPAVEQAMNK EFSAYLLENP
     QAAKSIAGKI IDAARARDAA RKAREMTRRK SALDIAGLPG KLAD
//
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