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P25714

- YIDC_ECOLI

UniProt

P25714 - YIDC_ECOLI

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Protein

Membrane protein insertase YidC

Gene

yidC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F0ATP synthase, FtsQ and SecE proteins and for Sec-independent subunit c of the F0ATP synthase, M13 phage procoat and the N-terminus of leader peptidase Lep. Probably interacts directly with Sec-independent substrates. Sec-dependent protein FtsQ interacts first with SecY then subsequently with YidC. Sec-dependent LacY and MalF require YidC to acquire tertiary structure and stability, a chaperone-like function, but not for membrane insertion. Stable maltose transport copmplex formation (MalFGK2) also requires YidC. Partially complements a Streptococcus mutans yidC2 disruption mutant.8 Publications

GO - Molecular functioni

  1. membrane insertase activity Source: EcoCyc

GO - Biological processi

  1. protein complex assembly Source: UniProtKB
  2. protein folding Source: UniProtKB
  3. protein homooligomerization Source: EcoCyc
  4. protein insertion into membrane Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:YIDC.
ECOL316407:JW3683-MONOMER.

Protein family/group databases

TCDBi2.A.9.3.1. the cytochrome oxidase biogenesis (oxa1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane protein insertase YidC
Alternative name(s):
Foldase YidC
Inner membrane protein YidC
Membrane integrase YidC
Oxa1Ec
Gene namesi
Name:yidC
Ordered Locus Names:b3705, JW3683
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11197. yidC.

Subcellular locationi

Cell inner membrane 2 Publications; Multi-pass membrane protein 2 Publications
Note: Predominantly localized at cell poles at all stages of cell growth.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicCurated
Transmembranei6 – 2318HelicalCuratedAdd
BLAST
Topological domaini24 – 342319PeriplasmicAdd
BLAST
Transmembranei343 – 37028HelicalCuratedAdd
BLAST
Topological domaini371 – 41646CytoplasmicAdd
BLAST
Transmembranei417 – 44630HelicalCuratedAdd
BLAST
Topological domaini447 – 46317PeriplasmicAdd
BLAST
Transmembranei464 – 48118HelicalCuratedAdd
BLAST
Topological domaini482 – 49312CytoplasmicAdd
BLAST
Transmembranei494 – 50916HelicalCuratedAdd
BLAST
Topological domaini510 – 5123Periplasmic
Transmembranei513 – 53523HelicalCuratedAdd
BLAST
Topological domaini536 – 54813CytoplasmicAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. integral component of plasma membrane Source: EcoCyc
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Lethality. Upon depletion experiments insertion of Sec translocase-independent integral membrane proteins ceases. Translocation of Sec-dependent protein decreases to a lesser extent. Also leads to decreased targeting and/or translocation of Lpp and BRP lipoproteins. Both spoIIIJ and yqjG of B.subtilis functionally complement yidC depletion, whereas Streptococcus mutans yidC1 and yidC2 only partially complement depletion.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 274EQDK → IEGR: Cold-sensitive at 30 degrees Celsius; when associated with 334-W--G-338. Protein accumulates stably.
Mutagenesisi334 – 3385WFISQ → LEVLFQG: Cold-sensitive at 30 degrees Celsius; when associated with 24-I--R-27. Protein accumulates stably. 1 Publication
Mutagenesisi361 – 3611I → S: Loss of function. 1 Publication
Mutagenesisi436 – 4361L → S: Loss of function. 1 Publication
Mutagenesisi483 – 4875PTTVT → LVPRGS: Temperature-sensitive at 42 degrees Celsius; when associated with 512-ENLYFQG. Protein is not stable. 1 Publication
Mutagenesisi512 – 5121G → ENLYFQG: Temperature-sensitive at 42 degrees Celsius; when associated with 483-L--S-487. Protein is not stable. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Membrane protein insertase YidCPRO_0000124712Add
BLAST

Proteomic databases

PaxDbiP25714.
PRIDEiP25714.

Expressioni

Inductioni

At mid-exponential phase in strain MC4100 there are about 2500 copies per cell (at protein level).

Gene expression databases

GenevestigatoriP25714.

Interactioni

Subunit structurei

Interacts with SecD and SecF. Component of the SecDFyajC complex, a heterotetrameric translocase complex. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration. Found in 3 different complexes in inner membrane preparations (PubMed:16079137). Can be cross-linked to FtsH, in the larger FtsH/HflKC complex.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VIIIP036235EBI-6400779,EBI-8482910From a different organism.

Protein-protein interaction databases

DIPiDIP-12442N.
IntActiP25714. 31 interactions.
MINTiMINT-6477960.
STRINGi511145.b3705.

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 645Combined sources
Beta strandi69 – 735Combined sources
Beta strandi78 – 9013Combined sources
Beta strandi95 – 1039Combined sources
Beta strandi106 – 11611Combined sources
Helixi123 – 1253Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi145 – 15410Combined sources
Beta strandi160 – 1689Combined sources
Beta strandi173 – 1819Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 20114Combined sources
Beta strandi220 – 2245Combined sources
Turni226 – 2283Combined sources
Beta strandi231 – 2333Combined sources
Helixi235 – 2395Combined sources
Beta strandi245 – 2506Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi260 – 28021Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi300 – 31112Combined sources
Helixi314 – 3207Combined sources
Helixi324 – 3274Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BLCX-ray2.50A/B26-340[»]
3BS6X-ray1.80A/B56-329[»]
4UTQelectron microscopy8.00A1-548[»]
ProteinModelPortaliP25714.
SMRiP25714. Positions 59-329, 352-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25714.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 264241Can be removed without causing lethality, dispensible for M13 procoat processingAdd
BLAST
Regioni215 – 26551Interacts with SecF; not required for insertion of a number of Sec-dependent or Sec-independent substratesAdd
BLAST
Regioni265 – 34682Required for Sec-dependent and Sec-independent protein insertionAdd
BLAST
Regioni527 – 54822Can be removed without causing lethality, dispensible for M13 procoat processingAdd
BLAST

Domaini

Most of the large periplasmic domain (residues 24-264) is not required for either Sec-dependent or Sec-independent protein insertion. However, residues 265-346, the C-terminal part of the large periplasmic domain, are required for both Sec-dependent and Sec-independent protein insertion.

Sequence similaritiesi

Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0706.
HOGENOMiHOG000101822.
InParanoidiP25714.
KOiK03217.
OMAiELTINTR.
OrthoDBiEOG6X6RF2.
PhylomeDBiP25714.

Family and domain databases

HAMAPiMF_01810. YidC_type1.
InterProiIPR019998. Membr_insert_YidC.
IPR028055. Membr_insert_YidC/Oxa1_C.
IPR028053. Membr_insert_YidC_N.
IPR001708. Membrane_insert_OXA1/ALB3/YidC.
[Graphical view]
PANTHERiPTHR12428. PTHR12428. 1 hit.
PfamiPF02096. 60KD_IMP. 1 hit.
PF14849. YidC_periplas. 1 hit.
[Graphical view]
PRINTSiPR00701. 60KDINNERMP.
PR01900. YIDCPROTEIN.
TIGRFAMsiTIGR03593. yidC_nterm. 1 hit.
TIGR03592. yidC_oxa1_cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

P25714-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSQRNLLVI ALLFVSFMIW QAWEQDKNPQ PQAQQTTQTT TTAAGSAADQ
60 70 80 90 100
GVPASGQGKL ISVKTDVLDL TINTRGGDVE QALLPAYPKE LNSTQPFQLL
110 120 130 140 150
ETSPQFIYQA QSGLTGRDGP DNPANGPRPL YNVEKDAYVL AEGQNELQVP
160 170 180 190 200
MTYTDAAGNT FTKTFVLKRG DYAVNVNYNV QNAGEKPLEI SSFGQLKQSI
210 220 230 240 250
TLPPHLDTGS SNFALHTFRG AAYSTPDEKY EKYKFDTIAD NENLNISSKG
260 270 280 290 300
GWVAMLQQYF ATAWIPHNDG TNNFYTANLG NGIAAIGYKS QPVLVQPGQT
310 320 330 340 350
GAMNSTLWVG PEIQDKMAAV APHLDLTVDY GWLWFISQPL FKLLKWIHSF
360 370 380 390 400
VGNWGFSIII ITFIVRGIMY PLTKAQYTSM AKMRMLQPKI QAMRERLGDD
410 420 430 440 450
KQRISQEMMA LYKAEKVNPL GGCFPLLIQM PIFLALYYML MGSVELRQAP
460 470 480 490 500
FALWIHDLSA QDPYYILPIL MGVTMFFIQK MSPTTVTDPM QQKIMTFMPV
510 520 530 540
IFTVFFLWFP SGLVLYYIVS NLVTIIQQQL IYRGLEKRGL HSREKKKS
Length:548
Mass (Da):61,526
Last modified:July 1, 1993 - v2
Checksum:i95EBC5DAB4F2FCFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10328 Genomic DNA. Translation: AAA62056.1.
U00096 Genomic DNA. Translation: AAC76728.1.
AP009048 Genomic DNA. Translation: BAE77588.1.
M11056 Genomic DNA. No translation available.
PIRiB65173.
RefSeqiNP_418161.1. NC_000913.3.
YP_491729.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76728; AAC76728; b3705.
BAE77588; BAE77588; BAE77588.
GeneIDi12932517.
948214.
KEGGiecj:Y75_p3467.
eco:b3705.
PATRICi32122907. VBIEscCol129921_3829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10328 Genomic DNA. Translation: AAA62056.1 .
U00096 Genomic DNA. Translation: AAC76728.1 .
AP009048 Genomic DNA. Translation: BAE77588.1 .
M11056 Genomic DNA. No translation available.
PIRi B65173.
RefSeqi NP_418161.1. NC_000913.3.
YP_491729.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BLC X-ray 2.50 A/B 26-340 [» ]
3BS6 X-ray 1.80 A/B 56-329 [» ]
4UTQ electron microscopy 8.00 A 1-548 [» ]
ProteinModelPortali P25714.
SMRi P25714. Positions 59-329, 352-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-12442N.
IntActi P25714. 31 interactions.
MINTi MINT-6477960.
STRINGi 511145.b3705.

Protein family/group databases

TCDBi 2.A.9.3.1. the cytochrome oxidase biogenesis (oxa1) family.

Proteomic databases

PaxDbi P25714.
PRIDEi P25714.

Protocols and materials databases

DNASUi 948214.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76728 ; AAC76728 ; b3705 .
BAE77588 ; BAE77588 ; BAE77588 .
GeneIDi 12932517.
948214.
KEGGi ecj:Y75_p3467.
eco:b3705.
PATRICi 32122907. VBIEscCol129921_3829.

Organism-specific databases

EchoBASEi EB1183.
EcoGenei EG11197. yidC.

Phylogenomic databases

eggNOGi COG0706.
HOGENOMi HOG000101822.
InParanoidi P25714.
KOi K03217.
OMAi ELTINTR.
OrthoDBi EOG6X6RF2.
PhylomeDBi P25714.

Enzyme and pathway databases

BioCyci EcoCyc:YIDC.
ECOL316407:JW3683-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25714.
PROi P25714.

Gene expression databases

Genevestigatori P25714.

Family and domain databases

HAMAPi MF_01810. YidC_type1.
InterProi IPR019998. Membr_insert_YidC.
IPR028055. Membr_insert_YidC/Oxa1_C.
IPR028053. Membr_insert_YidC_N.
IPR001708. Membrane_insert_OXA1/ALB3/YidC.
[Graphical view ]
PANTHERi PTHR12428. PTHR12428. 1 hit.
Pfami PF02096. 60KD_IMP. 1 hit.
PF14849. YidC_periplas. 1 hit.
[Graphical view ]
PRINTSi PR00701. 60KDINNERMP.
PR01900. YIDCPROTEIN.
TIGRFAMsi TIGR03593. yidC_nterm. 1 hit.
TIGR03592. yidC_oxa1_cterm. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Physical mapping and nucleotide sequence of the rnpA gene that encodes the protein component of ribonuclease P in Escherichia coli."
    Hansen F.G., Hansen E.B., Atlung T.
    Gene 38:85-93(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
    Strain: K12.
  5. "Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli."
    Saaf A., Monne M., de Gier J.W., von Heijne G.
    J. Biol. Chem. 273:30415-30418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
    Strain: K12/ MC1061 / TOP10F'.
  6. "YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase."
    Scotti P.A., Urbanus M.L., Brunner J., de Gier J.-W., von Heijne G., van der Does C., Driessen A.J.M., Oudega B., Luirink J.
    EMBO J. 19:542-549(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEC-DEPENDENT PATHWAY, INTERACTION WITH TRANSMEMBRANE SEGMENTS.
  7. Cited for: FUNCTION IN SEC-INDEPENDENT PATHWAY, SUBSTRATES, DISRUPTION PHENOTYPE.
  8. "Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC."
    Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.
    EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSQ AFTER SECY, DISRUPTION PHENOTYPE.
  9. Cited for: SRP- AND SEC-DEPENDENT INSERTION INTO MEMBRANES, SUBCELLULAR LOCATION, TOPOLOGY.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  10. "SecDFyajC forms a heterotetrameric complex with YidC."
    Nouwen N., Driessen A.J.M.
    Mol. Microbiol. 44:1397-1405(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SECD AND SECF.
  11. Cited for: FUNCTION.
  12. "Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YidC structural requirements for membrane protein insertion."
    Chen M., Xie K., Nouwen N., Driessen A.J., Dalbey R.E.
    J. Biol. Chem. 278:23295-23300(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 23-TRP--LYS-27; 334-TRP--GLN-338; 483-PRO--THR-487 AND GLY-512.
  13. "Defining the regions of Escherichia coli YidC that contribute to activity."
    Jiang F., Chen M., Yi L., de Gier J.-W.L., Kuhn A., Dalbey R.E.
    J. Biol. Chem. 278:48965-48972(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-361 AND LEU-436.
  14. "YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase."
    Yi L., Jiang F., Chen M., Cain B., Bolhuis A., Dalbey R.E.
    Biochemistry 42:10537-10544(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ATP SYNTHASE SUBUNIT AND SECE AS SUBSTRATES.
  15. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
    Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
    J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TARGETING AND/OR TRANSLOCATION OF LIPOPROTEINS.
  16. "Role of YidC in folding of polytopic membrane proteins."
    Nagamori S., Smirnova I.N., Kaback H.R.
    J. Cell Biol. 165:53-62(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FOLDING BUT NOT INSERTION OF LACY, DISRUPTION PHENOTYPE.
  17. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  18. "Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity."
    Xie K., Kiefer D., Nagler G., Dalbey R.E., Kuhn A.
    Biochemistry 45:13401-13408(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PERIPLASMIC DOMAIN.
  19. "Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins."
    van Bloois E., Dekker H.L., Froderberg L., Houben E.N., Urbanus M.L., de Koster C.G., de Gier J.W., Luirink J.
    FEBS Lett. 582:1419-1424(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSH.
  20. "Functional overlap but lack of complete cross-complementation of Streptococcus mutans and Escherichia coli YidC orthologs."
    Dong Y., Palmer S.R., Hasona A., Nagamori S., Kaback H.R., Dalbey R.E., Brady L.J.
    J. Bacteriol. 190:2458-2469(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPLEMENTATION BY AND IN STREPTOCOCCUS MUTANS.
  21. "Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC."
    Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M., Genevaux P., Luirink J., de Gier J.W.
    J. Biol. Chem. 283:17881-17890(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FOLDING BUT NOT INSERTION OF MALF OR OF MALFGK(2) COMPLEX.
  22. "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis."
    Saller M.J., Fusetti F., Driessen A.J.
    J. Bacteriol. 191:6749-6757(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPLEMENTATION BY SPOIIIJ AND YQJG OF B.SUBTILIS.
  23. "Membrane localization of small proteins in Escherichia coli."
    Fontaine F., Fuchs R.T., Storz G.
    J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  24. "Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC."
    Oliver D.C., Paetzel M.
    J. Biol. Chem. 283:5208-5216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-340.
    Strain: K12.
  25. "The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft."
    Ravaud S., Stjepanovic G., Wild K., Sinning I.
    J. Biol. Chem. 283:9350-9358(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 56-329.
  26. "Assembly of bacterial inner membrane proteins."
    Dalbey R.E., Wang P., Kuhn A.
    Annu. Rev. Biochem. 80:161-187(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiYIDC_ECOLI
AccessioniPrimary (citable) accession number: P25714
Secondary accession number(s): Q2M818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3