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Y338_CHLMU
ID   Y338_CHLMU              Reviewed;         326 AA.
AC   Q9PKX2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-SEP-2021, entry version 109.
DE   RecName: Full=Uncharacterized metal-binding lipoprotein TC_0338;
DE   Flags: Precursor;
GN   OrderedLocusNames=TC_0338;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Part of an ATP-driven transport system
CC       TC_0338/TC_0339/TC_0341/TC_0342 for a metal. Metal-binding component.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000305}.
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DR   EMBL; AE002160; AAF39201.1; -; Genomic_DNA.
DR   PIR; F81714; F81714.
DR   RefSeq; WP_010904314.1; NC_002620.2.
DR   STRING; 243161.TC_0338; -.
DR   EnsemblBacteria; AAF39201; AAF39201; TC_0338.
DR   GeneID; 1246382; -.
DR   KEGG; cmu:TC_0338; -.
DR   PATRIC; fig|243161.6.peg.367; -.
DR   eggNOG; COG0803; Bacteria.
DR   HOGENOM; CLU_016838_1_1_0; -.
DR   OMA; DPHIWFD; -.
DR   OrthoDB; 1703187at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_4.
DR   InterPro; IPR006127; ZnuA-like.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Metal-binding; Palmitate; Signal;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000305"
FT   CHAIN           22..326
FT                   /note="Uncharacterized metal-binding lipoprotein TC_0338"
FT                   /id="PRO_0000031899"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  36984 MW;  330B3072EB2B83A4 CRC64;
     MFFLHVRKYK HVIGGLLCLA GCFVISSCSS GRGNKSIDER IHILSMNRMI YDCVSRITGD
     RVKNIVLIDG SIDPHSYEMV KGDEDRMAIS QLIFCNGLGL EHSASLRKHL EGNSKVIDLG
     ARLLDKNCFV LLSEDGFPDP HIWTDMGVWI SXVKEMASVL VQQIPQYAEE FQKNAEQILS
     EMEDLDRWAV RSLATIPEKN RYLVTGHNAF SYFTRRYLSS DEERESGNWK LRCMSPEGLS
     PEAQISIRDI MRVVEYICAN DVGVVFLEDT LNQDALRKIV SCSKSGQKIR LAKSPLYSDN
     VCDNYFNTFQ HNVRTITEEL GGTVLE
 
 
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