ID   YIDC_LEPBL              Reviewed;         622 AA.
AC   Q04XE2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Membrane protein insertase YidC {ECO:0000255|HAMAP-Rule:MF_01810};
DE   AltName: Full=Foldase YidC {ECO:0000255|HAMAP-Rule:MF_01810};
DE   AltName: Full=Membrane integrase YidC {ECO:0000255|HAMAP-Rule:MF_01810};
DE   AltName: Full=Membrane protein YidC {ECO:0000255|HAMAP-Rule:MF_01810};
GN   Name=yidC {ECO:0000255|HAMAP-Rule:MF_01810}; OrderedLocusNames=LBL_2936;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L550;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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. {ECO:0000255|HAMAP-Rule:MF_01810}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01810}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01810}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01810}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01810}.
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DR   EMBL; CP000348; ABJ80253.1; -; Genomic_DNA.
DR   RefSeq; WP_011671159.1; NC_008508.1.
DR   AlphaFoldDB; Q04XE2; -.
DR   SMR; Q04XE2; -.
DR   KEGG; lbl:LBL_2936; -.
DR   HOGENOM; CLU_016535_3_0_12; -.
DR   OMA; LWAICER; -.
DR   OrthoDB; 524437at2; -.
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   TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Membrane; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..622
FT                   /note="Membrane protein insertase YidC"
FT                   /id="PRO_1000070117"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01810"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01810"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01810"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01810"
FT   TRANSMEM        571..591
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01810"
FT   REGION          33..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  70798 MW;  DA2FE8F5313DDF8D CRC64;
     MEDRQSRLFL ALILSMGIWM GVNYFFFPPT PKKTSETKEV KVDKPSDDKQ DQIQKEKKES
     RTTIPSKGTK IIPSESKKTL VVTESYIVEF SSLGGRISKF YVKDFTGPNG ELVQVARKDP
     ETLIVDGKTY YGVELSREKG FDFNFTDSLN ELPHSEWNRI PFSLAENKAD HSVVFSAFSP
     DKTYQLKKTF RFFDRENYFK VTVSVINLTK EKLSFASQKN VQYLRTFGSL GPFPKDRPLN
     DRDTANFFRF YHLDGSFNDT LDGSSSVGFW SSIVNFFTGN SGVDESFSLK TSTGGVDFAG
     TGSRYFIAVA DPLDHKPQGI ILDNRPKNES GAVLVYNNIT LGPGEVYNLD FASYVGIRES
     IGMVFHDPEL DPSQTKNSPF AGLSSDLNKS FNQGITTPFR NGIIWVLKQI YRFTIPNYGW
     SIIIFAILFK LVFYPLNQKQ AESMKKMQEL SPQLKTINEK FANDPKMRQQ KTMELYKKNN
     VNPVGGCLPM VIQIPIFIAL YTAFSDTIDL WNSPFLWVKD LSEPDVIWTS PAIPYFTQTG
     IGLNLLALLM VGTQIFQTRM TSVSMDPNQK MLMYVMPVMM LYIFWNMPSG VTLYWTFQNV
     LSIGQQWVTN HLKKTEAKKK AV