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YIDC2_ALKHC
ID   YIDC2_ALKHC             Reviewed;         280 AA.
AC   Q9KDP2;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Membrane protein insertase YidC 2 {ECO:0000255|HAMAP-Rule:MF_01811};
DE   AltName: Full=Foldase YidC 2 {ECO:0000255|HAMAP-Rule:MF_01811};
DE   AltName: Full=Membrane integrase YidC 2 {ECO:0000255|HAMAP-Rule:MF_01811};
DE   AltName: Full=Membrane protein YidC 2 {ECO:0000255|HAMAP-Rule:MF_01811};
DE   Flags: Precursor;
GN   Name=yidC2 {ECO:0000255|HAMAP-Rule:MF_01811}; OrderedLocusNames=BH1169;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(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. {ECO:0000255|HAMAP-Rule:MF_01811}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01811};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01811}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01811}.
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DR   EMBL; BA000004; BAB04888.1; -; Genomic_DNA.
DR   PIR; A83796; A83796.
DR   PDB; 3WO6; X-ray; 2.40 A; A=27-266.
DR   PDB; 3WO7; X-ray; 3.20 A; A/B=27-267.
DR   PDBsum; 3WO6; -.
DR   PDBsum; 3WO7; -.
DR   AlphaFoldDB; Q9KDP2; -.
DR   SMR; Q9KDP2; -.
DR   STRING; 272558.10173785; -.
DR   TCDB; 2.A.9.3.6; the membrane protein insertase (yidc/alb3/oxa1) family.
DR   DNASU; 892166; -.
DR   EnsemblBacteria; BAB04888; BAB04888; BAB04888.
DR   KEGG; bha:BH1169; -.
DR   eggNOG; COG0706; Bacteria.
DR   HOGENOM; CLU_036138_5_0_9; -.
DR   OMA; QWPILIA; -.
DR   Proteomes; UP000001258; 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   HAMAP; MF_01811; YidC_type2; 1.
DR   InterPro; IPR028055; Membr_insert_YidC/Oxa1_C.
DR   InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR   InterPro; IPR023060; YidC/YidC1/YidC2_Firmicutes.
DR   PANTHER; PTHR12428; PTHR12428; 1.
DR   Pfam; PF02096; 60KD_IMP; 1.
DR   TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW   Protein transport; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   CHAIN           23..280
FT                   /note="Membrane protein insertase YidC 2"
FT                   /id="PRO_0000020376"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   HELIX           29..40
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           42..55
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           60..103
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           111..128
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           132..135
FT                   /evidence="ECO:0007829|PDB:3WO7"
FT   HELIX           138..155
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   TURN            157..161
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           176..193
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           224..235
FT                   /evidence="ECO:0007829|PDB:3WO6"
FT   HELIX           238..255
FT                   /evidence="ECO:0007829|PDB:3WO6"
SQ   SEQUENCE   280 AA;  32108 MW;  724F78BC47E7C270 CRC64;
     MNYMKRRLLL FAGILLLVAL AGCSTTDPIT SESEGIWNHF FVYPMSWLIT TVANLLNGSY
     GLSIIIVTIL IRLALLPLTL KQQKSMRAMQ VIRPEMEAIQ KKYKEKGSKD PKVQQEMQKE
     LLGLYQKHGV NPMAGCLPLF IQLPILMAFY FAIMRTEEIR YHTFLWFDLG QPDYILPFVA
     GITTYFQFKM TMSHQQQMQK TNPSDSDNPM ANMMQMQMKV MLYVMPVMII IAGLSLPSAL
     SLYWVIGNIF MIIQTYFIVV KAPPLEVEQT KQKSSKPNKA
 
 
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