ID W6TBC6_9LACO Unreviewed; 863 AA.
AC W6TBC6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=LFAB_00030 {ECO:0000313|EMBL:ETY75763.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY75763.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY75763.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY75763.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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:ETY75763.1}.
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DR EMBL; AWWK01000001; ETY75763.1; -; Genomic_DNA.
DR RefSeq; WP_051385255.1; NZ_KK036455.1.
DR AlphaFoldDB; W6TBC6; -.
DR STRING; 1400520.LFAB_00030; -.
DR PATRIC; fig|1400520.3.peg.6; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000019247; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 16..469
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 808..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..537
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 827..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 863 AA; 95343 MW; 3B4A7071A07D57F7 CRC64;
MKDLADADLP TRITDVNLSK TMRTSFLSYA MSVIVARALP DVRDGLKPVH RRILYGMSEL
GVTPDKPYKK SARIVGDVMG KYHPHGDSAI YESMVRMAQD FSYRYMLVDG HGNFGSVDGD
GAAAMRYTEA RMSKIAVEML RDINKDTVDW QPNYDDTERE PAVLPARFPN LLVNGATGIA
VGMTTNIPPH NLSEVISAIH LLMDNPDATT ADLMEVLPGP DFPTGGIVMG KSGIRKAYEH
GRGNIIIRAK VDIQEQKNGK QRIIVTELPY MVNKAKLIER IASLARDKEI EGITDINDES
DREGMRVVID VRRDASASVI LNNLYKMTLM QTNYGFNMLA IVKGAPKVLS LKQILIYYLE
HQEDVIRRRT QFDLKKAQAR AHILEGLRIA LDHIDEIITI IRQSQTSEIA KNQLMENYGL
SDKQAQAILD MRLVRLTGLE REKIESEYQD LLKAIADYKA ILASRERINQ IIYEELLEIQ
RKFGDKRRTE LMVGEVLSIE DEDLIEEEEV AVTLTHNGYI KRLPTTEFKS QHRGGRGIQG
MDVHDDDFIE HLLTTSTHDV LLFFTNAGKV YRMKAYEIPE YGRTAKGIPV INLLGVNSGE
KIQAVVNVSG DADDSDKFLF FTTVKGVVKR TPVQEFSNIR SNGLKAITLK DDDELIGVTV
TDGSQNVIIG THDGYAVSFD ETTVRSMGRT AAGVRGIRLR DDDFVIGFDI LKPDSKVFII
TEKGYGKQTP AAEYPIKGRG GKGIKTANVT DKNGHLAGLT TVEGAEDIMV MTDQGVMIRF
GISTVSQTGR ATLGVRLIRL TGDGKVATMA KVDPEPEEAE TAAATDATTP DGESVPASTA
ETTEPTGTPA PADGDTDDTT DEN
//
