ID   YIDC2_STRP8             Reviewed;         307 AA.
AC   Q8P2D8;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
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};
GN   OrderedLocusNames=spyM18_0404;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97148.1; -; Genomic_DNA.
DR   RefSeq; WP_002985918.1; NC_003485.1.
DR   AlphaFoldDB; Q8P2D8; -.
DR   SMR; Q8P2D8; -.
DR   KEGG; spm:spyM18_0404; -.
DR   HOGENOM; CLU_036138_5_1_9; -.
DR   OMA; GWAIIII; -.
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   3: Inferred from homology;
KW   Cell membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW   Protein transport; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   CHAIN           24..307
FT                   /note="Membrane protein insertase YidC 2"
FT                   /id="PRO_0000020417"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        209..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   REGION          263..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01811"
SQ   SEQUENCE   307 AA;  34530 MW;  E45EA2328ED4BA76 CRC64;
     MKLTLNRILF SGLALSILFT LTGCVGRDAH GNPKGMIWEF LGKPMSYFID YFANNAGLGY
     GLAIIIVTII VRTLILPLGL YQSWKASYQS EKMTFLKPVF EPINKRIKQA SSQEEKMAAQ
     TELMAAQRAH GINPLGGIGC LPLLIQMPFF SAMYFAAQYT KGVSTSTFMG IDLGSRSLVL
     TAIIAALYFF QSWLSMMAVS EEQREQMKTM MYTMPIMMIF MSFSLPAGVG LYWLVGGFFS
     IIQQLITTYL LKPRLHKQIK EEYAKTPPKA YQSTSSRKDV TPSQNMEQAN LPKKIKSNRN
     AGKQRKR