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Database: UniProt
Entry: C6W539_DYAFD
LinkDB: C6W539_DYAFD
Original site: C6W539_DYAFD 
ID   C6W539_DYAFD            Unreviewed;       602 AA.
AC   C6W539;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Membrane protein insertase YidC {ECO:0000256|ARBA:ARBA00015325, ECO:0000256|HAMAP-Rule:MF_01810};
DE   AltName: Full=Foldase YidC {ECO:0000256|ARBA:ARBA00033342, ECO:0000256|HAMAP-Rule:MF_01810};
DE   AltName: Full=Membrane integrase YidC {ECO:0000256|ARBA:ARBA00033245, ECO:0000256|HAMAP-Rule:MF_01810};
DE   AltName: Full=Membrane protein YidC {ECO:0000256|HAMAP-Rule:MF_01810};
GN   Name=yidC {ECO:0000256|HAMAP-Rule:MF_01810};
GN   OrderedLocusNames=Dfer_1150 {ECO:0000313|EMBL:ACT92399.1};
OS   Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS   52180 / NS114).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT92399.1, ECO:0000313|Proteomes:UP000002011};
RN   [1] {ECO:0000313|EMBL:ACT92399.1, ECO:0000313|Proteomes:UP000002011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC   {ECO:0000313|Proteomes:UP000002011};
RX   PubMed=21304649; DOI=10.4056/sigs.19262;
RA   Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA   Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL   Stand. Genomic Sci. 1:133-140(2009).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01810}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01810}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01810}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010527, ECO:0000256|HAMAP-Rule:MF_01810}.
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DR   EMBL; CP001619; ACT92399.1; -; Genomic_DNA.
DR   RefSeq; WP_015810653.1; NC_013037.1.
DR   AlphaFoldDB; C6W539; -.
DR   STRING; 471854.Dfer_1150; -.
DR   KEGG; dfe:Dfer_1150; -.
DR   eggNOG; COG0706; Bacteria.
DR   HOGENOM; CLU_016535_2_0_10; -.
DR   OrthoDB; 9780552at2; -.
DR   Proteomes; UP000002011; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032977; F:membrane insertase activity; IEA:InterPro.
DR   GO; GO:0051205; P:protein insertion into membrane; IEA:UniProt.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd20070; 5TM_YidC_Alb3; 1.
DR   CDD; cd19961; EcYidC-like_peri; 1.
DR   Gene3D; 2.70.98.90; -; 1.
DR   HAMAP; MF_01810; YidC_type1; 1.
DR   InterPro; IPR019998; Membr_insert_YidC.
DR   InterPro; IPR028053; Membr_insert_YidC_N.
DR   InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR   InterPro; IPR028055; YidC/Oxa/ALB_C.
DR   InterPro; IPR047196; YidC_ALB_C.
DR   InterPro; IPR038221; YidC_periplasmic_sf.
DR   NCBIfam; TIGR03593; yidC_nterm; 1.
DR   NCBIfam; TIGR03592; yidC_oxa1_cterm; 1.
DR   PANTHER; PTHR12428:SF65; INNER MEMBRANE PROTEIN ALBINO3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR12428; OXA1; 1.
DR   Pfam; PF02096; 60KD_IMP; 1.
DR   Pfam; PF14849; YidC_periplas; 1.
DR   PRINTS; PR00701; 60KDINNERMP.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01810};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01810};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01810};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01810};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01810}; Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01810};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01810};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01810}.
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01810"
FT   TRANSMEM        412..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01810"
FT   TRANSMEM        469..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01810"
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01810"
FT   DOMAIN          68..333
FT                   /note="Membrane insertase YidC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14849"
FT   DOMAIN          349..546
FT                   /note="Membrane insertase YidC/Oxa/ALB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02096"
FT   REGION          38..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  68287 MW;  183DE1DD5560DE12 CRC64;
     MDKNFVIGLV LIMLMLIGYQ ILVPKPVEPT PVAEVKKEVS KPSSVTSDTT QNSSQSVDSL
     AIPQKDLVIE TKDARVVFTN KGGVMKEVML KNYKTYDQKP LYLIAENHNK FQIDLPTQTG
     DVRLTNQTFT TDAQDRTLAE GDSAVITYRA TIKNNQTVEQ TYVVRGTGYV IDYGIKASGA
     LPANKSVEFH WDNDLLQLEN DMKKNREVVT VNYYTDELKS LATSPTSNEE EKTADPVKWF
     TIKHKYFLAG LIAEKHPLTN VTVRANVNPE DSVIVKNMNV FAGIPTAAVQ KGEANFQFYL
     GPNEYHIVDK VKAENFDQNV YLGYAFLKPI NKFFLVPLFN LIEGFVSNYG LLIILLVLFV
     KTLLTPLTYK SYISMAKMRI LGPELEQIRE QNKDDLAKQQ QEQMKLYQQV GVSPLSGCVP
     VLATMPILFS LFFLFPNLIE LRQQSFLWAD DLSTYDSFFK LPFEVPFGIG NHISLFTILM
     TASSIGYAYY NNQNTPTQPG PVNMKALGYV MPLMFMFILN SFPAGLTFYY FVSNVVTIAQ
     QLLIKRFVNE DKIKNILEEN RKKNATGEKK QSKFQKYLEK SLQAAEEAKK KQAELEKKTK
     KK
//
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