ID A0A1Z9AL13_9GAMM Unreviewed; 748 AA.
AC A0A1Z9AL13;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CBC55_06985 {ECO:0000313|EMBL:OUV21124.1};
OS Gammaproteobacteria bacterium TMED95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1986771 {ECO:0000313|EMBL:OUV21124.1, ECO:0000313|Proteomes:UP000195745};
RN [1] {ECO:0000313|EMBL:OUV21124.1, ECO:0000313|Proteomes:UP000195745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED95 {ECO:0000313|EMBL:OUV21124.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUV21124.1}.
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DR EMBL; NHEW01000023; OUV21124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9AL13; -.
DR Proteomes; UP000195745; 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; 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; 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 13..463
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 125
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 44
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 80
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 124
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 748 AA; 83011 MW; 658D48DEB321A325 CRC64;
MTEVQDLNNI ENQSLAEFTE NAYLNYAMYV INDRALPHIG DGLKPVQRRI IYAMSELRLN
ADAKYMKSAR TIGDVIGKYH PHGDSASYEA MVLMAQNFTY RYPLVDGQGN WGSPDDPKSY
AAMRYTESKL TQYSKVLLSE LGQGTVEWIA NFDGTMEEPV VLPARLPNLL LNGGTGIAVG
MATDILPHNL NEIVSACVHL LDAPKATVAD LMTHVKGPDF PTGAEIISTP AEIQQCYESG
RGSVRARAVY QIEAGEIVIE ALPYQVSGTK ILEQIASQMQ AKKLPMVVDL RDESDHENPT
RIVIVPRSNR VDLVALMSHL FASTDLERTY RVNQNVIQLD GRPGVCSLKE LLSQWLTYRQ
QTVLKRLQFR LEKILDRLHL LEGLMIAFLN IDEVIQIIRS EDKPKQILMS RFDLSDRQAE
AILDLRLRQL AKLEEIKIKG EQDELMAERQ TLEQTIGSKA RLKTLIKKEL LADAEVFGDA
RRSAIVTRAE AKAFSERDLL TSDPITVVLS QNGWIRAAKG HEVKVQELSY RTGDAYLASA
TGKTNQTAIF LDSTGRSYAL AAHTLPSARG QGEPLTGKIN PPAGSQFTGV IIDEIDQKYL
IASDAGYGFI GRVEDMISKN KAGKAYLSVP NGAASLPACP VDNPETQLIA AFTSQGRLLI
FPATELPELA RGKGNKIINI PSAAVKSREE VMAHVLVFSE KDSITVFSGK RHIHLTLKEL
THYRGERARR GLKLPRGFQK VDRVVLNR
//
