ID C6M5Y6_NEISI Unreviewed; 769 AA.
AC C6M5Y6;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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:EET44214.1};
GN ORFNames=NEISICOT_01936 {ECO:0000313|EMBL:EET44214.1};
OS Neisseria sicca ATCC 29256.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=547045 {ECO:0000313|EMBL:EET44214.1, ECO:0000313|Proteomes:UP000005365};
RN [1] {ECO:0000313|EMBL:EET44214.1, ECO:0000313|Proteomes:UP000005365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET44214.1,
RC ECO:0000313|Proteomes:UP000005365};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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:EET44214.1}.
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DR EMBL; ACKO02000011; EET44214.1; -; Genomic_DNA.
DR RefSeq; WP_003758760.1; NZ_ACKO02000011.1.
DR AlphaFoldDB; C6M5Y6; -.
DR STRING; 490.A6J88_01365; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000005365; 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 16..488
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 47
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 85
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 769 AA; 84776 MW; 11A9B68099B6D7AA CRC64;
MNEHVSVPSP VGEDYLLLGQ YAERAYLEYA MSVVKGRALP EVSDGQKPVQ RRILFAMRDM
GLTAGAKPVK SARVVGEILG KYHPHGDSSA YEAMVRMAQD FTLRYPLIDG IGNFGSRDGD
GAAAMRYTEA RLTPIAELLL SEINQGTVDF VPNYDGAFDE PLHLPARLPM VLLNGASGIA
VGMATEIPSH NLNEVTQAAI ALLKKPTLET ADLMQYIPAP DFAGGGQIIT PADELRRIYE
TGKGSVRVRA RYEIEKLARG QWRVIVTELP PNANSAKILA EIEEQTNPKP KAGKKQLNQD
QLNTKKLMLD LIDRVRDESD GEHPVRLVFE PKSSRIDTDT FINTLMAQTS LEGNVSMNLV
MMGLDNRPAQ KNLKTILQEW LDFRVVTVTR RLKFRLNQVE KRLHILEGRL KVFLHIDEVI
KVIRESDDPK TDLMAAFGLT EIQAEDILEI RLRQLARLEG FKLEKELNEL REEQGRLNIL
LGDENEKRKL IIKEMQADMK QFGDARRTLV EEAGRAVLTQ TTADEPITLI LSEKGWIRSR
AGHNLDLSQT AFKEGDRLKQ TLEGRTVLPV VILDSLGRTY TLDAAEIPGG RGDGVPVSSL
IELQNGAKPV AMLTGQPEQH YLLSGSGGYG FITKLGDMVG RVKAGKVVMT VDSGETVLPP
IAVYASSLIN PDCKIVLASS DHRLLAFSIG ELKVMPKGRG LQLMSLTEGA SLEHVLVTTA
AEFIVETVGK RGAAHQEKLR ICDIEGKRGK KGKVLDISGR LKTLSAASE
//
