ID C4GCC6_9FIRM Unreviewed; 882 AA.
AC C4GCC6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 ECO:0000313|EMBL:EEP28068.1};
GN ORFNames=GCWU000342_01615 {ECO:0000313|EMBL:EEP28068.1};
OS Shuttleworthia satelles DSM 14600.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Shuttleworthia.
OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28068.1, ECO:0000313|Proteomes:UP000003494};
RN [1] {ECO:0000313|EMBL:EEP28068.1, ECO:0000313|Proteomes:UP000003494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28068.1,
RC ECO:0000313|Proteomes:UP000003494};
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 (APR-2009) 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:EEP28068.1}.
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DR EMBL; ACIP02000003; EEP28068.1; -; Genomic_DNA.
DR AlphaFoldDB; C4GCC6; -.
DR STRING; 626523.GCWU000342_01615; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000003494; 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:UP000003494};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 21..479
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 821..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 540..546
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 848..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 882 AA; 98767 MW; 0E5AB9B784A9D569 CRC64;
MAEMGDDIFD QTVRSDTIQE VDLKSTMETS YIDYAMSVIA ARALPDVRDG LKPVQRRVLY
SMIELNNTPD KPHRKCARIV GDTMGKYHPH GDSSIYGALV NMAQPWSMRN ILVDGHGNFG
SIDGDGAAAM RYTEARLSKI SMAMMADINK DTVDFIPNFD ETEKEPVVLP ARLPNLLVNG
TTGIAVGMAT NIPPHNLREV IAACVKIIDN RVEEDRSTDI SEILGIVKGP DFPTGGIILG
RAGIEEAYRT GRGKIKVRAV ADIEPMDNGK HRIIVSEIPY GVNKARMIEK IADMVKDKRL
DGITALRDET SREGMRVVIE LRKDINPNVM LNKLYKQTQL QDSYGVIMLA LVGNQPRIMS
LKEVLDHYIL HQEDVVTRRT RFDLNKAQER DHILQGLLTA LDNIDEVIKI IRSSKSVAIA
KEQLMGRFAL SEAQAQAIVD MRLRALTGLE REKLEAEHRE LMEKIAYFKG ILADHKKLLT
VVKEEMQEIA DKYGDDRRTQ IGFDDDDISA EDLIPVTHPI ITFTKFGYIK RMSADNFRAQ
HRGGKGIKGM ETIKDDYIVE LIQTRSHNFL YFFTNKGRVY RLKAYEIPEA SRTARGTAIV
NLLQLMPDET ITSMIPVVPG EDEDKYLFMA TQRGIVKKTR LREYENIRKS GLAAINLRDE
DRLIEVKLTD DTDEVMLFTR FGQCVRFHES DVRGTGRSTM GVIGINLSDQ DCVIAMQLAS
QGESLVLVSQ RGLGKCTLTE EFPSHHRGGK GVKCYKITEK TGDLVGVKSV DKDNQLMLIN
RAGTIIRINI ADTALLGRIT SGVKLIDLKG DDEVASISVV QREDLPLEDE DTSESMGDGL
PVDSDQAREN QESADADHSL EDLLVRAEED QSAREDDSEE EE
//
