ID A0A084J7K2_9CLOT Unreviewed; 847 AA.
AC A0A084J7K2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=IO99_17505 {ECO:0000313|EMBL:KEZ84936.1};
OS Clostridium sulfidigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ84936.1, ECO:0000313|Proteomes:UP000028542};
RN [1] {ECO:0000313|EMBL:KEZ84936.1, ECO:0000313|Proteomes:UP000028542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113A {ECO:0000313|EMBL:KEZ84936.1,
RC ECO:0000313|Proteomes:UP000028542};
RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT "Draft genome of Clostridium sulfidigenes 113A isolated from sediments
RT associated with methane hydrate from Krishna Godavari basin.";
RL Submitted (JUL-2014) 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:KEZ84936.1}.
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DR EMBL; JPMD01000051; KEZ84936.1; -; Genomic_DNA.
DR RefSeq; WP_035135500.1; NZ_JPMD01000051.1.
DR AlphaFoldDB; A0A084J7K2; -.
DR STRING; 318464.IO99_17505; -.
DR GeneID; 84602735; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000028542; 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; 6.
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:UP000028542};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 10..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 808..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 829..847
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 847 AA; 95152 MW; 9A477258C8DE4EE4 CRC64;
MDTIDKIIPV DIEKEMKKSY IDYAMSVIVG RALPDVRDGL KPVHRRILYS MHELGITYEK
GYRKCARIVG DVLGKYHPHG DSSVYDALVR MAQSFSIRYM LVDGHGNFGS VDGDGAAAMR
YTEAKMSKIT SQMLRDINKE TVDFKPNFDG EEKEPEVLPA RFPTLLVNGS SGIAVGMATN
IPPHNLTEVI NAVIMLIDNP DVTVSDFMSE IKGPDFPTGG IILGKSGIRS AYETGRGKVL
VRSKAEIEEH KGRNRIIVTE IPYMVNKANL IESIANLVKE KKIDGISDLR DESDRDGMRI
VIELKRDANA NVVLNRLYKH TKMQDTFGII MLALVDNEPK VLNLKQILTH YLNHQRDVIT
RRTIFDLDKA NARAHILEGL RIALDHIDAV ISLIRASKTT QEAKEGLIEK FNLSEKQAQA
ILDLKLQRLT GLERDKIEDE YNELMKTIAY LQSILNSEEI LLNIIKDELV EIKTKYGDDR
RTLIEKNPYS FEDEDLIDDD DIVITLTHGG YIKRLPADTY NAQKRGGRGI QGVTTKEDDF
VEHILITPTL NNILFFTNKG KVYKLKGYEI PEGGRTAKGT NIVNMLPLDP DENIQAVMSI
RTFDSDNYLL MGTKSGMVKK TSLDKFENIR KNGLNAINLK EDDEIVGVRI TKGDDEVLFV
TKYGYSIRFS EKEVRNMGRT TTGVKAITLR DDDIAVSMII AKPDEELLVI SEKGFGKRTA
IENYTLQRRG GKGIKTYKIS EKTGNVVSAR VVRDVDEIML INSNGIIIRI NVSDISTTSR
NAMGVTLMKT GEDVNIVAVA KINYNSEEEK NEDKQMSIDG IVDNENNLSE NLDESDDLEE
SDDKTLE
//
