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YIDC_CHLMU
ID   YIDC_CHLMU              Reviewed;         787 AA.
AC   Q9PKE3;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Membrane protein insertase YidC;
DE   AltName: Full=Foldase YidC;
DE   AltName: Full=Membrane integrase YidC;
DE   AltName: Full=Membrane protein YidC;
DE   Flags: Precursor;
GN   Name=yidC; OrderedLocusNames=TC_0522;
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: Required for the insertion and/or proper folding and/or
CC       complex formation of integral membrane proteins into the membrane.
CC       Involved in integration of membrane proteins that insert both
CC       dependently and independently of the Sec translocase complex, as well
CC       as at least some lipoproteins. Aids folding of multispanning membrane
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the Sec translocase complex via SecD.
CC       Specifically interacts with transmembrane segments of nascent integral
CC       membrane proteins during membrane integration (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE002160; AAF39364.1; -; Genomic_DNA.
DR   PIR; G81692; G81692.
DR   AlphaFoldDB; Q9PKE3; -.
DR   SMR; Q9PKE3; -.
DR   STRING; 243161.TC_0522; -.
DR   EnsemblBacteria; AAF39364; AAF39364; TC_0522.
DR   KEGG; cmu:TC_0522; -.
DR   eggNOG; COG0706; Bacteria.
DR   HOGENOM; CLU_019734_0_0_0; -.
DR   OMA; LNIYWLS; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032977; F:membrane insertase activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.98.90; -; 1.
DR   HAMAP; MF_01810; YidC_type1; 1.
DR   InterPro; IPR019998; Membr_insert_YidC.
DR   InterPro; IPR028055; Membr_insert_YidC/Oxa1_C.
DR   InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR   InterPro; IPR038221; YidC_periplasmic_sf.
DR   PANTHER; PTHR12428; PTHR12428; 1.
DR   Pfam; PF02096; 60KD_IMP; 1.
DR   PRINTS; PR01900; YIDCPROTEIN.
DR   TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Lipoprotein; Membrane;
KW   Palmitate; Protein transport; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..787
FT                   /note="Membrane protein insertase YidC"
FT                   /id="PRO_0000124704"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        636..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        735..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   787 AA;  87736 MW;  CC259BA941FDEDA2 CRC64;
     MRMNKRTLLF VSLVSAAFLG CQIFFGYQDL KSCQDLAEKQ RAISEQILAS TEQLSVVPWT
     ASAEESESVN QYAVRLGNRL LVLTKGGAHS EVHSKGTSWK LIDQTSTFGG ILVSLYGEDG
     QEVLSKGGSV YLPNQQDALP VLVAEFRRNQ EPLVFFGEYK NGKLSNKAGT IYGTSLVFLN
     TGNEFVPLGI YNSKEECVES LDLPMARAVV FADKENLTTS GSYYMLANEY MQVIVSQESG
     AIEGINLPFA SDREGNKSIV NEIGFDRELA AGSPSEASFP GVQAIDSQRQ NVSSVVGGYY
     PLLRRGTLSD TRKMVSPQYQ ALNIVSGREL SSPVATGFRV VSFDNKTLVL ESGDGGIRKT
     YTLGEQPYAF DLEIQTTRGQ EDLWITSGVP EVEIMSNAFV PAVKYHAVKK NKSDLINVKL
     PKAKDSLLVR NDASPQWILN SNGYFGVILT PKTPLPTGYA SSFIPGNAVP TRLTQLSPKD
     QAYPASKYPG YTAMLPLPKE AGRYQFMVYA GPLSEPTLKA LDRAHTNHKG ESPEYVDAIA
     FRGFFSFITE PFAALLFIIM KFFQFLTGSW GISIILLTIV LKLVLYPLNA WSIRSMRRMQ
     KLSPYIQDIQ QKYKREPKRA QMEIMALYKV NKVNPITGCL PLIIQIPFLI AMFDLLKSSF
     LLRGASFIPG WIDNLTAPDV LFSWETPIWF IGKEFHLLPI LLGIVMFAQQ KISAIKRSGP
     VSDQQRQQEA MGTMMALLFT FMFYNFPSGL NIYWLSSMLL GVIQQWATNK ILDEKHLQHE
     VIVNKKR
 
 
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