YIDC1_STRMU
ID YIDC1_STRMU Reviewed; 271 AA.
AC Q8DVX3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Membrane protein insertase YidC 1;
DE AltName: Full=Foldase YidC 1;
DE AltName: Full=Membrane integrase YidC 1;
DE AltName: Full=Membrane protein YidC 1;
DE Flags: Precursor;
GN Name=yidC1; OrderedLocusNames=SMU_337;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=NG8;
RX PubMed=16293689; DOI=10.1073/pnas.0508778102;
RA Hasona A., Crowley P.J., Levesque C.M., Mair R.W., Cvitkovitch D.G.,
RA Bleiweis A.S., Brady L.J.;
RT "Streptococcal viability and diminished stress tolerance in mutants lacking
RT the signal recognition particle pathway or YidC2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17466-17471(2005).
RN [3]
RP COMPLEMENTATION BY AND IN E.COLI.
RC STRAIN=NG8;
RX PubMed=18178746; DOI=10.1128/jb.01366-07;
RA Dong Y., Palmer S.R., Hasona A., Nagamori S., Kaback H.R., Dalbey R.E.,
RA Brady L.J.;
RT "Functional overlap but lack of complete cross-complementation of
RT Streptococcus mutans and Escherichia coli YidC orthologs.";
RL J. Bacteriol. 190:2458-2469(2008).
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 (By similarity). Partially complements an
CC E.coli yidC depletion experiment. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16293689}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014133; AAN58096.1; -; Genomic_DNA.
DR RefSeq; NP_720790.1; NC_004350.2.
DR RefSeq; WP_002264887.1; NC_004350.2.
DR AlphaFoldDB; Q8DVX3; -.
DR SMR; Q8DVX3; -.
DR STRING; 210007.SMU_337; -.
DR PRIDE; Q8DVX3; -.
DR DNASU; 1027894; -.
DR EnsemblBacteria; AAN58096; AAN58096; SMU_337.
DR KEGG; smu:SMU_337; -.
DR PATRIC; fig|210007.7.peg.292; -.
DR eggNOG; COG0706; Bacteria.
DR HOGENOM; CLU_036138_5_0_9; -.
DR OMA; WIMPIMI; -.
DR PhylomeDB; Q8DVX3; -.
DR Proteomes; UP000002512; 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 PRINTS; PR00701; 60KDINNERMP.
DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..271
FT /note="Membrane protein insertase YidC 1"
FT /id="PRO_0000020404"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
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 271 AA; 31326 MW; 39AAB88F13444564 CRC64;
MKKKYRIIGL AVAALLFLSA CGRSQVTSHS SDAWEKFVYF FAETIRFLSI NGRIGIGIIL
FTFLIRTILL PLFNLQLKSG QKMQELQPEL KALQTKYPGK DRESRMRMAE ESQELYKKYG
VNPYASLFPL LIQMPVLWAL YQALTRVEFL KTGSFLWMDI GNKDPYFILP VLAAIFTFLS
SWLTNKAAKE RNGMMITMNI ILPIFILLIG FNLASGVALY WVVSNAYQVF QILLLNNPFK
IIAERQRLED EARELEAKKR RAKKKAHKKR K