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Y1019_STRR6
ID   Y1019_STRR6             Reviewed;         279 AA.
AC   Q8DPT4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=DegV domain-containing protein spr1019;
GN   OrderedLocusNames=spr1019;
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 [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).
CC   -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and may
CC       play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
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DR   EMBL; AE007317; AAK99823.1; -; Genomic_DNA.
DR   PIR; C97999; C97999.
DR   RefSeq; NP_358613.1; NC_003098.1.
DR   RefSeq; WP_000161389.1; NC_003098.1.
DR   PDB; 6NR1; X-ray; 2.10 A; A/B=1-279.
DR   PDBsum; 6NR1; -.
DR   AlphaFoldDB; Q8DPT4; -.
DR   SMR; Q8DPT4; -.
DR   STRING; 171101.spr1019; -.
DR   EnsemblBacteria; AAK99823; AAK99823; spr1019.
DR   GeneID; 60233939; -.
DR   KEGG; spr:spr1019; -.
DR   PATRIC; fig|171101.6.peg.1109; -.
DR   eggNOG; COG1307; Bacteria.
DR   HOGENOM; CLU_048251_3_2_9; -.
DR   OMA; EIHAKIN; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1180.10; -; 1.
DR   InterPro; IPR003797; DegV.
DR   InterPro; IPR043168; DegV_C.
DR   Pfam; PF02645; DegV; 1.
DR   TIGRFAMs; TIGR00762; DegV; 1.
DR   PROSITE; PS51482; DEGV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lipid-binding; Reference proteome.
FT   CHAIN           1..279
FT                   /note="DegV domain-containing protein spr1019"
FT                   /id="PRO_0000209798"
FT   DOMAIN          4..277
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         62
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT   BINDING         94
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           16..22
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           48..55
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           96..106
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          111..115
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           120..135
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          154..161
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          183..192
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          195..204
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           207..218
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          224..233
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          254..257
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   HELIX           260..266
FT                   /evidence="ECO:0007829|PDB:6NR1"
FT   STRAND          271..277
FT                   /evidence="ECO:0007829|PDB:6NR1"
SQ   SEQUENCE   279 AA;  30668 MW;  E013F05826E545E8 CRC64;
     MTKIKIVTDS SVTIEPELVK QLDITIVPLS VMIDNVVYSD ADLKEEGKFL QLMQESKNLP
     KTSQPPVGVF AEIFEDLCKD GGQILAIHMS HALSGTVEAA RQGASLSTAD VIVVDSSFTD
     QALKFQVVEA AKLAQEGKDM EAILSHVEEV KNHTELYIGV STLENLVKGG RIGRVTGLLS
     SLLNIRVVMQ MKDHELQPMV KGRGTKTFKK WLDELITSLS ERAVAEIGIS YSGSDDWAKE
     MKESLQAYVE KPISVLETGS IIQTHTGENA WAILIRYHS
 
 
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