(data stored in SCRATCH9089 zone)

SWISSPROT: A0KPK2_AERHH

ID   A0KPK2_AERHH            Unreviewed;       764 AA.
AC   A0KPK2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00936};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
GN   Name=parC {ECO:0000256|HAMAP-Rule:MF_00936,
GN   ECO:0000313|EMBL:ABK37982.1};
GN   OrderedLocusNames=AHA_3755 {ECO:0000313|EMBL:ABK37982.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37982.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37982.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC       relaxes supercoiled DNA. Performs the decatenation events required
CC       during the replication of a circular DNA molecule. {ECO:0000256|HAMAP-
CC       Rule:MF_00936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00936,
CC         ECO:0000256|SAAS:SAAS01218217};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00936}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00936}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}.
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DR   EMBL; CP000462; ABK37982.1; -; Genomic_DNA.
DR   RefSeq; WP_011707468.1; NC_008570.1.
DR   RefSeq; YP_858203.1; NC_008570.1.
DR   STRING; 380703.AHA_3755; -.
DR   EnsemblBacteria; ABK37982; ABK37982; AHA_3755.
DR   GeneID; 4489621; -.
DR   KEGG; aha:AHA_3755; -.
DR   PATRIC; fig|380703.7.peg.3727; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076277; -.
DR   KO; K02621; -.
DR   OMA; PRSNRID; -.
DR   BioCyc; AHYD380703:G1G7B-3752-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_00936; ParC_type1; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR005742; TopoIV_A_Gneg.
DR   Pfam; PF03989; DNA_gyraseA_C; 2.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KPK2.
DR   SWISS-2DPAGE; A0KPK2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00936,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00936, ECO:0000256|SAAS:SAAS00972514,
KW   ECO:0000313|EMBL:ABK37982.1}; Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00936,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN          15..465
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          433..453
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        127
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            46
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            82
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            84
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT   SITE            126
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   764 AA;  84745 MW;  1E404196AD6AA933 CRC64;
     MSDAIELSLD GVERQPMRTF TEQAYLNYSM YVIMDRALPH IGDGLKPVQR RIIYAMSELG
     LSALSKHKKS ARTVGDVLGK YHPHGDSACY EAMVLMAQPF SYRYPLVDGQ GNWGAPDDPK
     SFAAMRYTEA RLSRFSELLL SELGQGTVEW TPNFDGTMKE PVVLPARLPH ILLNGVTGIA
     VGMATDIPPH NAREVAHACV ELLDNPNAGL DALMAHVQGP DYPTNAEIIT PRDDIRKIYE
     TGKGSIKQRA VWNEEDGDIV ITALPHQASG AKIMEQIAAQ MVAKKLPMVT DLRDESDHEN
     PTRLVIVPRS NRVDVEGLMA HLFATTDLEK NYRVNLNILG LDNRPQVKDL KTILTEWLSF
     RRETVRRRLQ YRLDKVLARL HILEGLLIAY LNIDEVIEII RTEEEPGRVM MERFNISEAQ
     AEAILELKLR HLAKLEEFKL RAEQNELAEE RDKLELILGS ERRLSTLLKK EILADAEKYG
     DDRRTPLVER ATAVALTEKE LTPSEPVTVI LSDKGWVRAA KGHDVDVEGL SYKAGDNYLA
     HAHGRSNQQA VFLSTLGRTY SLEAHTLPSA RSQGEPLTGR FALGAGEEVR HLVMGNEGEP
     YLICSDAGYG FVCKYDDLIG KNKNGKALLT VPEGGLVMAP QKIGAPDTDL CMAISNEGRM
     LLFPLNTLPV LGKGKGNKLI SIPSARVKAR EEFVVMAAVI PQGQSVTLFA GKRKLTLKPA
     DLDYYRGERG RRGAKLPRGL QRVDRIEIET VAGAEPAAGE NQEG
//

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