YIDC2_STRMU
ID YIDC2_STRMU Reviewed; 310 AA.
AC Q8DSP8;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Membrane protein insertase YidC 2;
DE AltName: Full=Foldase YidC 2;
DE AltName: Full=Membrane integrase YidC 2;
DE AltName: Full=Membrane protein YidC 2;
DE Flags: Precursor;
GN Name=yidC2; OrderedLocusNames=SMU_1727;
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: Doubling time increases for growth under
CC nonstress conditions, unable to initiate growth at pH 5.0 and under
CC 3.5% NaCl salt stress. Double deletions of yidC2 and SRP (signal
CC recognition particle) components are barely able to grow in the absence
CC of stress. E.coli yidC partially complements this disruption.
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; AAN59360.1; -; Genomic_DNA.
DR RefSeq; NP_722054.1; NC_004350.2.
DR RefSeq; WP_002262549.1; NC_004350.2.
DR AlphaFoldDB; Q8DSP8; -.
DR SMR; Q8DSP8; -.
DR STRING; 210007.SMU_1727; -.
DR PRIDE; Q8DSP8; -.
DR EnsemblBacteria; AAN59360; AAN59360; SMU_1727.
DR KEGG; smu:SMU_1727; -.
DR PATRIC; fig|210007.7.peg.1543; -.
DR eggNOG; COG0706; Bacteria.
DR HOGENOM; CLU_036138_5_1_9; -.
DR OMA; GWAIIII; -.
DR PhylomeDB; Q8DSP8; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..310
FT /note="Membrane protein insertase YidC 2"
FT /id="PRO_0000020405"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 263..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 34908 MW; 635C588871D6F49F CRC64;
MKKIYKRLLF SGLALSMLFF LSGCVQMKNG KPTGEGWVYK FFAAPMGSVI QYLANNLGLG
FGFAIIIVTV IVRLLILPLG LSQVRKMTYQ SEKMAYLKPV FDPIQERMKN AKTQEEKMAA
QTELMQAQRH YGMSMFGGLG CLPLLIQMPF FSALYISTRY TKGIASASFL GIKLGSPNMI
ITVIIGILYL VQSWVSTLSV PEAQRQQTRN MMFMMPIMMV MISIGAPAGG ALYWLVSGIF
GLIQQLITNH IIKPKLRKQI DEEFKKNPPK PFKSNARKDI TPQANNDKKL ITSKKQKSNR
NAGKQRHHKQ
