ID A0A0P1GVL3_9RHOB Unreviewed; 782 AA.
AC A0A0P1GVL3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:CUH79061.1};
GN ORFNames=TRM7557_02182 {ECO:0000313|EMBL:CUH79061.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH79061.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH79061.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH79061.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_00936};
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; CYSD01000033; CUH79061.1; -; Genomic_DNA.
DR RefSeq; WP_058290227.1; NZ_JAQIPA010000011.1.
DR AlphaFoldDB; A0A0P1GVL3; -.
DR STRING; 928856.SAMN04488049_1103; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000052022; Unassembled WGS sequence.
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; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR005742; TopoIV_A_Gneg.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 3.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00936};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00936};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 21..495
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 52
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 782 AA; 87496 MW; 0AFC693573B30CA6 CRC64;
MSELVDDPEH PELPEEGEIL EPLRRAIGER YLTYALSTIM HRALPDARDG LKPVHRRILY
AMSRLRLTSS GGFLKSAKIS GDTMGDFHPH GDAAIYDAMA RLAQDFNVRY PLVDGQGNFG
NIDGDNPAAS RYTEARMTFI AEAMLQGLAE DAVDFRDNYD GRLQEPAVLP ATFPNILANG
ASGIAVGMAT NIPPHNIAEL IDACIHLIKS PGAADDTLLQ YVPGPDFPTG GVIVEPKENI
AEAYRKGRGS FRLRSTWEVE DLGRGQWQVV VTEIPYQVQK SKLIEKIAEL IQTKKVPILA
DIRDESADDI RIVLEPKSKN VDPELLMGMM FRNSDLEIRF SLNMNVLIDG VTPKVCSMKE
VLRAFLDHRR DVLQRRSRHR MGKIDHRLEV LDGFIIAFLN LDRVIDIIRY DEDPKAALMR
EDWDREHPRA FSEDDYQTPL PGAGELSEVQ AEAILNMRLR SLRKLEEIEL TRERDALREE
RAGLVELLGS EDLQWKRITE QLRDTKKQFG KDYAGGARRT RFAEAGEVEE VPIEAMIERE
PITVVCSQMG WIRAMTGHID LTRELKFKDG DGPRFIFHAE TTDRLLVFAS NGRVFTVSAA
NLPGGRGMGE PLRLMVDLPN EAEIVDILIH RPEGKLLVAS DAGNGFICAE ADIVAQTRGG
KQVLNVKDDE RAKICIPVSG DHVAVVSENG KFLTFAIEEM PELNRGKGVR LQKYNMARGK
QGALELDGGL SDVTTFTWAE GLSWEMGGGK TRHEPDLSEW LGKRGSVGKR PPYGFPKNYK
FK
//
