ID U5P398_9STRE Unreviewed; 818 AA.
AC U5P398;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=N597_03935 {ECO:0000313|EMBL:AGY38103.1};
OS Streptococcus ilei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38103.1, ECO:0000313|Proteomes:UP000017124};
RN [1] {ECO:0000313|EMBL:AGY38103.1, ECO:0000313|Proteomes:UP000017124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA Hyun D.-W.;
RT "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT fluid.";
RL Submitted (SEP-2013) 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; CP006776; AGY38103.1; -; Genomic_DNA.
DR RefSeq; WP_023023148.1; NC_022582.1.
DR AlphaFoldDB; U5P398; -.
DR STRING; 1156433.N597_03935; -.
DR KEGG; sip:N597_03935; -.
DR PATRIC; fig|1156433.3.peg.751; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000017124; 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};
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 818 AA; 91349 MW; B311CC2693F9C5A8 CRC64;
MQDNNLVDVN LTSEMKTSFI DYAMSVIVSR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRYML VDGHGNFGSM DGDGAAAQRY
TEARMSKIAL EMLRDINKNT VDFTDNYDAS EREPNVLPAR FPNLLVNGAT GIAVGMATNI
PPHNLGESID AVKLMMDNPD VTTRELMEVL PGPDFPTGAL VMGKSGIHKA YETGKGSIVL
RSRTEIEETK TGRERIVVTE FPYMVNKTKV HEHIVRLVQE KRIDGITAVR DESNREGVRF
VIEVRRDASA NVILNNLFKM TQMQTNFGFN MLAIQNGVPK ILSLREILGS YIEHQKEVVT
RRTIFDKEKA EARAHILEGL LIALDHIDEV IKIIRNSQTD AEAQAELMSK FKLSERQSQA
ILDMRLRRLT GLERDKIQSE YDDLIALIAD LADILAKPER VATIIKEELD EVKRKFGDAR
RTELMVGEVL SLEDEDLIEE TDVLITLSNK GYIKRLDQAE FTAQKRGGRG VQGTGVKDDD
FVRELVSTST HDRLLFFTNK GRVYRLKGYE IPEYGRTAKG LPIVNLLKLD DGESIQTIIN
VAQDRSEDSY LFFTTRSGLV KRTSVAEFAN IRQNGLKALN LKDEDELINV FLTDGNADVI
IGTKFGYSVR FKESVVRNMG RSATGVRGVN LRPGDQVVGA SVITDQDEVL IITEKGYGKR
TRADEYPTKG RGGKGIKTAN VAEKNGPLAG LMTVKGDEDL MIITNTGVMI RTSVANISQT
GRSTMGVKVM RLDQDAQIVT FTTVQADEKD ESETESEG
//
