ID A0A1M5X670_9GAMM Unreviewed; 757 AA.
AC A0A1M5X670;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=SAMN02745129_3245 {ECO:0000313|EMBL:SHH95068.1};
OS Ferrimonas marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=299255 {ECO:0000313|EMBL:SHH95068.1, ECO:0000313|Proteomes:UP000184268};
RN [1] {ECO:0000313|EMBL:SHH95068.1, ECO:0000313|Proteomes:UP000184268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16917 {ECO:0000313|EMBL:SHH95068.1,
RC ECO:0000313|Proteomes:UP000184268};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQXG01000005; SHH95068.1; -; Genomic_DNA.
DR RefSeq; WP_067660993.1; NZ_FQXG01000005.1.
DR AlphaFoldDB; A0A1M5X670; -.
DR STRING; 299255.SAMN02745129_3245; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000184268; 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; 1.
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:UP000184268};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 15..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..453
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 480..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 757 AA; 84774 MW; 97B6E7ED724D06FC CRC64;
MTDLSEMSLE GVEQLPLRQF TEQAYLNYSM YVIMDRALPF IGDGLKPVQR RIIYAMSELG
LSATAKYKKS ARTVGDVLGK YHPHGDSACY EAMVLMAQPF TYRYPLVDGQ GNWGAPDDPK
SFAAMRYTES RLSRFSEVLL SELGQGTVEW GPNFDGTLKE PKTMPARLPH ILLNGITGIA
VGMATDIPPH NAREVANACA HLLEHPKAEL AELMEFVQGP DYPTEAEIIT PRSDIEKLYR
TGKGSIKMRA VYSIQDGEVV ITALPHQVSG AKLIEQIAAQ MQAKKLPMVA DLRDESDHEN
PVRLVVVPRS NRIDLDQLMA HLFATTDLEK SFRVNLNMLG LDNRPGVRDL KSILVEWLQF
RTETVRRRLQ YRLDKVLTRL HILDGLLIAF LNIDEVIDII RNEDEPKAAL MARFDLSEKQ
AEAILEIKLR QLAKLEEMKI RGEQEELAKE RDKLELILGS ERRLKTLVRK ELLADAETYG
DDRRSPLQER EESKAMSEQD LTPAEAVTVV MSEKAWGRCA KGHEVDPTAL SYRAGDGYLA
HARGKSNQPV VFLESSGRAY TTEPHTLPSA RSQGEPMSGR FNLVAGARLE HVVMGQESDL
YLMASDAGYG FICQYKDMIS RNKAGKALLT VPVGAEVLAP QRIEDQGSQR LLAVTTEGRM
LLFPLSQLPV LAKGKGNKII GIPGERAKSR EEYLKHLVVL SEQARITLWA GKRKLTLKPD
DLAHYLGERG RRGNKLPRGL QRVDRVEIEQ DQPATDA
//
