ID F7NSP1_9GAMM Unreviewed; 756 AA.
AC F7NSP1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=Rhein_0775 {ECO:0000313|EMBL:EGM79156.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79156.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM79156.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM79156.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(2011).
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:EGM79156.1}.
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DR EMBL; AFHI01000005; EGM79156.1; -; Genomic_DNA.
DR RefSeq; WP_008897667.1; NZ_AFHI01000005.1.
DR AlphaFoldDB; F7NSP1; -.
DR STRING; 506534.Rhein_0775; -.
DR eggNOG; COG0188; Bacteria.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000004282; 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 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 14..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 45
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 125
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 756 AA; 83903 MW; 672D721E419CE6DE CRC64;
MTDIMISNEG TEQLPLRRFT EEAYLNYSMY VIMDRALPFI GDGLKPVQRR IIYAMSELGL
SHLAKYKKSA RTVGDVLGKF HPHGDSACYE AMVLMAQPFS YRYPLVDGQG NWGAPDDPKS
FAAMRYTEAK LSRFSEVLLN ELGQGTVDWV PNFDGTLDEP RTLPARLPHI LLNGVTGIAV
GMATDIPPHN AREVANATAF LLDNPKATIP DLMQYIQGPD YPTDAEIISP AHELQAIYET
GRGSIKMRGL YQLEDGDIII TALPHQTSGS KVLEQIAAQM NAKKLPMVSD LRDESDHENP
TRIVIVPRSN RIDVEQLMAH LFATTDLEKS YRVNLNILGL DQRPRVKNLL EILSEWLVFR
RDTVRRRLQF RLDKVLDRLH VLEALLIAFL NIDEVIKIIR ENDQPKPVLM AHFGITERQA
EAILELKLRH LAKLEEMKIR GEQAELEKER DYLEGILGSE KKLTKLIREE LLADAEKYGD
NRRSPIVMRE EAKALSEKEL LPSEPVTVVL SEKGWVRCAK GHDIDGNSLQ YKAGDGFKAA
ASGRSNRYAA FIDSSGRSFA AEAHDLPSAR GQGEPLTGRF TLVAGENFEH VLMAEDSQKL
LLASDAGYGF VGTFADLVSR NKAGKAVLTL PTGAKVLAPI PIKNPETDLV VAISTEGRML
VFPVADLPQL SKGKGNKILS IPSARAASRE EYLKLLTVVP AATAVTLVAG KRKMTIKVDD
LAHYIGERGR RGNKLPRGLQ RIDELLTGEV AGDTTE
//