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GYRA_STRR6
ID   GYRA_STRR6              Reviewed;         822 AA.
AC   Q8DPM2;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=spr1099;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9603872; DOI=10.1128/jb.180.11.2854-2861.1998;
RA   Balas D., Fernandez-Moreira E., de la Campa A.G.;
RT   "Molecular characterization of the gene encoding the DNA gyrase A subunit
RT   of Streptococcus pneumoniae.";
RL   J. Bacteriol. 180:2854-2861(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-145.
RA   Janoir C.;
RL   Submitted (SEP-1996) 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:0000255|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:0000255|HAMAP-
CC         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:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR   EMBL; AF053121; AAC23563.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAK99902.1; -; Genomic_DNA.
DR   EMBL; Y07845; CAA69173.1; -; Genomic_DNA.
DR   PIR; B98009; B98009.
DR   RefSeq; NP_358692.1; NC_003098.1.
DR   RefSeq; WP_001152994.1; NC_003098.1.
DR   PDB; 4Z2C; X-ray; 3.19 A; A/B=1-493.
DR   PDB; 4Z2D; X-ray; 3.38 A; A/B=1-493.
DR   PDB; 4Z2E; X-ray; 3.46 A; A/B=1-493.
DR   PDB; 6N1P; EM; 6.35 A; A/B/C/D/E/F/G/H=1-487.
DR   PDB; 6N1Q; EM; 5.16 A; A/B/C/D/E/F/G/H=1-487.
DR   PDB; 6N1R; EM; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-487.
DR   PDBsum; 4Z2C; -.
DR   PDBsum; 4Z2D; -.
DR   PDBsum; 4Z2E; -.
DR   PDBsum; 6N1P; -.
DR   PDBsum; 6N1Q; -.
DR   PDBsum; 6N1R; -.
DR   AlphaFoldDB; Q8DPM2; -.
DR   SMR; Q8DPM2; -.
DR   STRING; 171101.spr1099; -.
DR   EnsemblBacteria; AAK99902; AAK99902; spr1099.
DR   GeneID; 60233881; -.
DR   KEGG; spr:spr1099; -.
DR   PATRIC; fig|171101.6.peg.1194; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   OMA; THHWLLF; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 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   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
FT   CHAIN           1..822
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145263"
FT   MOTIF           524..530
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        120
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   CONFLICT        537
FT                   /note="K -> E (in Ref. 1; AAC23563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        618..620
FT                   /note="GIV -> VLL (in Ref. 1; AAC23563)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           11..29
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   TURN            35..38
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           41..53
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           80..89
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           129..133
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   TURN            134..139
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          149..156
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           163..167
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           185..197
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           203..207
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           225..233
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          234..241
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          243..248
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:4Z2E"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           267..278
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          286..291
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           310..320
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          324..330
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          338..341
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           344..385
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           387..395
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           400..411
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           415..422
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           426..429
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           433..456
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   HELIX           458..476
FT                   /evidence="ECO:0007829|PDB:4Z2C"
FT   STRAND          482..485
FT                   /evidence="ECO:0007829|PDB:4Z2C"
SQ   SEQUENCE   822 AA;  92039 MW;  130307B8B5160EAD CRC64;
     MQDKNLVNVN LTKEMKASFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
     HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRYML VDGHGNFGSM DGDSAAAQRY
     TEARMSKIAL EMLRDINKNT VDFVDNYDAN EREPLVLPAR FPNLLVNGAT GIAVGMATNI
     PPHNLGETID AVKLVMDNPE VTTKDLMEVL PGPDFPTGAL VMGKSGIHKA YETGKGSIVL
     RSRTEIETTK TGRERIVVTE FPYMVNKTKV HEHIVRLVQE KRIEGITAVR DESNREGVRF
     VIEVKRDASA NVILNNLFKM TQMQTNFGFN MLAIQNGIPK ILSLRQILDA YIEHQKEVVV
     RRTRFDKEKA EARAHILEGL LIALDHIDEV IRIIRASETD AEAQAELMSK FKLSERQSQA
     ILDMRLRRLT GLERDKIQSE YDDLLALIAD LADILAKPER VSQIIKDELD EVKRKFSDKR
     RTELMVGQVL SLEDEDLIEE SDVLITLSNR GYIKRLDQDE FTAQKRGGRG VQGTGVKDDD
     FVRELVSTST HDHLLFFTNK GRVYRLKGYE IPEYGRTAKG LPVVNLLKLD EDESIQTVIN
     VESDRSDDAY LFFTTRHGIV KRTSVKEFAN IRQNGLKALN LKDEDELINV LLAEGDMDII
     IGTKFGYAVR FNQSAVRGMS RIATGVKGVN LREGDTVVGA SLITDQDEVL IITEKGYGKR
     TVATEYPTKG RGGKGMQTAK ITEKNGLLAG LMTVQGDEDL MIITDTGVMI RTNLANISQT
     GRATMGVKVM RLDQDAQIVT FTTVAVAEKE EVGTENETEG EA
 
 
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