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ENGB_STAA1
ID   ENGB_STAA1              Reviewed;         196 AA.
AC   A7X395;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=SAHV_1660;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC       normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00321};
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00321}.
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DR   EMBL; AP009324; BAF78543.1; -; Genomic_DNA.
DR   RefSeq; WP_000867697.1; NZ_CTYB01000017.1.
DR   AlphaFoldDB; A7X395; -.
DR   SMR; A7X395; -.
DR   KEGG; saw:SAHV_1660; -.
DR   HOGENOM; CLU_033732_3_0_9; -.
DR   OMA; LMMDIRH; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   CDD; cd01876; YihA_EngB; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00321; GTPase_EngB; 1.
DR   InterPro; IPR030393; G_ENGB_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03598; GTPase_YsxC; 1.
DR   PROSITE; PS51706; G_ENGB; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; GTP-binding; Magnesium; Metal-binding;
KW   Nucleotide-binding; Septation.
FT   CHAIN           1..196
FT                   /note="Probable GTP-binding protein EngB"
FT                   /id="PRO_1000005860"
FT   DOMAIN          24..196
FT                   /note="EngB-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         77..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         176..178
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ   SEQUENCE   196 AA;  22685 MW;  04CEA96C45193332 CRC64;
     MKVNPNNIEL IISAVKEEQY PETELSEVAL SGRSNVGKST FINSMIGRKN MARTSQQPGK
     TQTLNFYNID EQLIFVDVPG YGYAKVSKTQ REKFGKMIEE YITKRENLQL VIQLVDLRHD
     PTQDDILMYN YLKHFDIPTL VICTKEDKIP KGKVQKHIKN IKTQLDMDPD DTIVSYSSIQ
     NNKQQQIWNL IEPYIS
 
 
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