ID A0A1S1Y892_9GAMM Unreviewed; 744 AA.
AC A0A1S1Y892;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=BJL95_17820 {ECO:0000313|EMBL:OHX37622.1};
OS Methylomonas sp. LWB.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1905845 {ECO:0000313|EMBL:OHX37622.1, ECO:0000313|Proteomes:UP000180009};
RN [1] {ECO:0000313|EMBL:OHX37622.1, ECO:0000313|Proteomes:UP000180009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LWB {ECO:0000313|EMBL:OHX37622.1,
RC ECO:0000313|Proteomes:UP000180009};
RA Stephenson J., Kumaresan D., Hillebrand-Voiculescu A.M., Murrell J.C.;
RT "Draft genome sequence of the methane oxidising bacterium Candidatus
RT Methylomonas sp. LWB isolated from Movile Cave.";
RL Submitted (OCT-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHX37622.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKMC01000008; OHX37622.1; -; Genomic_DNA.
DR RefSeq; WP_071155711.1; NZ_MKMC01000008.1.
DR AlphaFoldDB; A0A1S1Y892; -.
DR Proteomes; UP000180009; 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 NCBIfam; TIGR01062; parC_Gneg; 1.
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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000180009};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 10..460
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 428..459
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 41
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 744 AA; 82308 MW; EC3378734BAB5F9D CRC64;
MGVQENFETL PLKDFTEKAY LDYSMYVILD RALPHIGDGL KPVQRRIVYA MSELGLTALA
KYKKSARTVG DVLGKYHPHG DSACYEAMVL MAQDFSYRYP LIDGQGNWGS PDDPKSFAAM
RYTESRLTAY AQTLLSELGQ GTVDWVDNFD GTLEEPSLLP ARLPNVLLNG TTGIAVGMAT
DIPPHNLREV AAAVLQLLDE PETPLESLLT HIKGPDFPTD AEIVTPAADL QKLYLTGNGS
VKMRAKYEVE DGNIVITALP HQVSGAKLLE QIAAQMLAKK LPMIEDLRDE SDHENPTRLL
IIPKTKRTDV DAVMSHLFAT TDLEKNFRVN LNMIGLNGKP QVKNLRQILT EWISFRTETV
RRRLQFRLDK VLARLHILEG LLIAYLNIDE VIAIIRREDH PKPVLMARFG LSDVQAEAIL
ELKLRHLAKL EEMKIRGEQD ELEREREELE KTLGSAHLLN RLIRKEIERD AEKYGDARRS
PIVAREAAQA LDTTELIANE PVTIILSQKG WIRAAKGYDI EVEGLSYRAG DGYLSSAKGR
TTLPAYVLDS TGRVYTITTH DLPSARSQGE PLTGRLNPPP GSIFTDVFTG QAEDWVLMSS
SAGYGFRVQL KELYGKNKAG KAVLTVPDKA EVMTPTPIPR DAEWLAVATL QGRLLIFPVA
DLPELAKGKG NKLIQIPSAD LASGKDAVVA VTALATRGEL KILSGKRFVT LKAIDIAQYS
GSRANRGNIL PRGFQKVDGL ESVV
//
