ID L1NXR4_9NEIS Unreviewed; 927 AA.
AC L1NXR4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=HMPREF9120_00832 {ECO:0000313|EMBL:EKY07982.1};
OS Neisseria sp. oral taxon 020 str. F0370.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY07982.1, ECO:0000313|Proteomes:UP000010457};
RN [1] {ECO:0000313|EMBL:EKY07982.1, ECO:0000313|Proteomes:UP000010457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0370 {ECO:0000313|EMBL:EKY07982.1,
RC ECO:0000313|Proteomes:UP000010457};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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_01897};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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:EKY07982.1}.
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DR EMBL; AMER01000071; EKY07982.1; -; Genomic_DNA.
DR RefSeq; WP_009425213.1; NZ_KB291075.1.
DR AlphaFoldDB; L1NXR4; -.
DR STRING; 1127694.HMPREF9120_00832; -.
DR PATRIC; fig|1127694.3.peg.774; -.
DR HOGENOM; CLU_002977_6_1_4; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000010457; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; 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_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
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 NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 7.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000010457};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 19..510
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 741..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 571..577
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 897..912
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 927 AA; 102646 MW; 8AF09DB0CF8CC493 CRC64;
MTDDTIRHDH KFALETLPVS LEDEMRKSYL DYAMSVIVGR ALPDVRDGLK PVHRRVLYAM
HELKNNWNAA YKKSARIVGD VIGKYHPHGD SAVYDTIVRM AQDFSMRYVL IDGQGNFGSV
DGDGAAAMRY TEIRMAKIAH EMLADIEEET VNFGPNYDGS EHEPLVLPTR FPALLVNGSS
GIAVGMATNI PPHNLTDTIN ACLRLLDEPE TEIDELINIL QAPDFPTGAT IYGLSGVREG
YKTGRGRVVM RGKTHIEPIG KNGEREAIII DEIPYQVNKA KLVEKIGELV REKTLEGVSD
LRDESDKSGM RVVIELKRNE NAEVVLNQLY KLTQLQDSFG INMVALVDGQ PRLLNLKQIL
AEFLRHRREV VTRRTLFRLK KARHEGHIAE GKAVALSNID EMIRLIKESA DAPEAKEKLL
SRAWRSGLVE DMLSRTDLDL RMARPEGLPA NLGLQEQGYY LSEIQADAIL RMSLRNLTGL
DQEEIVGDYK NIMAKIIDFL DILAKPERIT QIIREELEET KTNFGDERRS EINPFGGDIA
DEDLIPQREM VVTLTHGGYI KTQPTTDYQA QRRGGRGKQA AATKDEDFIE TLFVANTHDY
LMCFTNLGKC HWIKVYKLPE GGRNSRGRPI NNVIQLEEGE KVSAILAVRE FPEDQYVFFA
TAQGMVKKVQ LSAFKNVRSQ GIKAIALKEG DYLVGAAQTG GSDDIMLFSN LGKAIRFNEY
WEKSGNDEAE DADIETEISD DLEDETADNE NALPSGKHGV RPSGRGSGGL RGMRLPADGK
IVSLITFAPE AAQSDLQVLT ATANGYGKRT PIADYSRKNK GGQGNIAINT GERNGDLVAA
TLVGETDDLM LITSGGVLIR TKVEQIRETG RAAAGVKLIN LDEGEQLVSL ERVAEEPEDT
AAEDESDADT GALENEAENK GAEEAEE
//
