ID I1Z7F8_ACIPI Unreviewed; 284 AA.
AC I1Z7F8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 pittii (Acinetobacter genomosp. 3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=48296 {ECO:0000313|EMBL:AFJ15218.1};
RN [1] {ECO:0000313|EMBL:AFJ15218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T11BR1 {ECO:0000313|EMBL:AFJ15218.1};
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:AFJ15218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T11BR1 {ECO:0000313|EMBL:AFJ15218.1};
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; JN903852; AFJ15218.1; -; Genomic_DNA.
DR AlphaFoldDB; I1Z7F8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.30.565.10; 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:AFJ15218.1"
FT NON_TER 284
FT /evidence="ECO:0000313|EMBL:AFJ15218.1"
SQ SEQUENCE 284 AA; 31821 MW; AE1F0858BFAF1D8F CRC64;
ALSSKLHLII NRAGQVHEQE YHHGDPQYPL RVIGETDSSG TTVRFWPSEL TFSQTIFNVE
ILARRLRELS FLNAGVRIVL RDERINLEHV YDYEGGLSEF VKYINEGKTH LNEIFHFTAD
TENGIGVEVA LQWNESYQEN VRCFTNNIPQ KDGGTHLAGF RAALTRGLNQ YLENENILKK
EKVNVTGDDA REGLTAIISV KVPDPKFSSQ TKEKLVSSEV KPAVEQAMNK EFSAYLLENP
QAAKSIAGKI IDAARARDAA RKAREMTRRK SALDIAGLPG KLAD
//
