ID A0A2L0D3Y7_9STRE Unreviewed; 820 AA.
AC A0A2L0D3Y7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=C0J00_05120 {ECO:0000313|EMBL:AUW96525.1};
OS Streptococcus pluranimalium.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=82348 {ECO:0000313|EMBL:AUW96525.1, ECO:0000313|Proteomes:UP000238956};
RN [1] {ECO:0000313|EMBL:AUW96525.1, ECO:0000313|Proteomes:UP000238956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH11417 {ECO:0000313|EMBL:AUW96525.1,
RC ECO:0000313|Proteomes:UP000238956};
RA Hurst M.R.H.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AUW96525.1, ECO:0000313|Proteomes:UP000238956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH11417 {ECO:0000313|EMBL:AUW96525.1,
RC ECO:0000313|Proteomes:UP000238956};
RA Zhang J.-R., Hu G.-Z.;
RT "Whole genome sequencing analysis of Streptococcus pluranimalium isolated
RT from cattle infected mastitis in China.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; CP025536; AUW96525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0D3Y7; -.
DR KEGG; splr:C0J00_05120; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000238956; Chromosome.
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:UP000238956};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 9..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 524..530
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 820 AA; 91617 MW; 3BF1CEC33DA8B8D1 CRC64;
MEDKNLVSVN LTSEMKTSFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
HKKSARITGD VMGKYHPHGD SSIYDAMVRM AQWWSYRYML VDGHGNFGSM DGDGAAAQRY
TEARMSKIAL EMLRDINKNT VDFQDNYDGS EREPLVLPAR FPNLLVNGAT GIAVGMATNI
PPHNLGETID AVKLVMDNPE VTTRDLMEVL PGPDFPTGAM VMGKSGIHRA YETGKGSIVL
RSKTEIEVTK TGRERIVVTE FPYMVNKTKV HEHIVKLAQE KRIEGITAVR DESSREGVRF
VIEVKRDASA NVILNNLFKM TSLQTNFSFN MLAIEKGVPK ILTLRQILDN YIAHQKEVIV
RRTEFDKSKA ESRAHILEGL LIALDHLDEV IAIIRNSQTD SEAQAELMTR FDLSERQSQA
ILDMRLRRLT GLERDKIQSE YDELLKLIAD LADILAKPER VITIIKEELD EVKRKFNDDR
RTELMVGEVL SLEDEDLIEE EDVLITLSNK GYIKRLAQDE FRAQKRGGRG VQGTGVNDDD
FVSQLVSTST HDTLLFFTNL GRVYKLKGYE IPEYGRTAKG LPVVNLLKLD EGEFIQTMIN
ARKEDIKDYY FFFTTYAGVV KRVPTSEFDN IRQNGLKALT LKDNDQLINV LVTTGNDDII
IGTTAGYSVR FNESVVRSMG RVAAGVRGVK LRDEDYVVGA STITDDQEVL VVTEKGYGKR
TPAEEYPTKG RGGKGIKTAN ITDKNGALAG LVTVSGDEDV MLITNKGVVI RTNVSNISQT
GRSTMGVRLM RLEEASKLVT FALVEAETAD EPAEVVDTED
//
