ID YIDC_ECOLI Reviewed; 548 AA. AC P25714; Q2M818; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 27-MAR-2024, entry version 172. DE RecName: Full=Membrane protein insertase YidC; DE AltName: Full=Foldase YidC; DE AltName: Full=Inner membrane protein YidC; DE AltName: Full=Membrane integrase YidC; DE AltName: Full=Oxa1Ec; GN Name=yidC; OrderedLocusNames=b3705, JW3683; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7686882; DOI=10.1006/geno.1993.1230; RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.; RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: RT organizational symmetry around the origin of replication."; RL Genomics 16:551-561(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3. RC STRAIN=K12; RX PubMed=2415431; DOI=10.1016/0378-1119(85)90206-9; RA Hansen F.G., Hansen E.B., Atlung T.; RT "Physical mapping and nucleotide sequence of the rnpA gene that encodes the RT protein component of ribonuclease P in Escherichia coli."; RL Gene 38:85-93(1985). RN [5] RP TOPOLOGY. RC STRAIN=K12/ MC1061 / TOP10F'; RX PubMed=9804807; DOI=10.1074/jbc.273.46.30415; RA Saaf A., Monne M., de Gier J.W., von Heijne G.; RT "Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli."; RL J. Biol. Chem. 273:30415-30418(1998). RN [6] RP FUNCTION IN SEC-DEPENDENT PATHWAY, AND INTERACTION WITH TRANSMEMBRANE RP SEGMENTS. RX PubMed=10675323; DOI=10.1093/emboj/19.4.542; RA Scotti P.A., Urbanus M.L., Brunner J., de Gier J.-W., von Heijne G., RA van der Does C., Driessen A.J.M., Oudega B., Luirink J.; RT "YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a RT component of the Sec translocase."; RL EMBO J. 19:542-549(2000). RN [7] RP FUNCTION IN SEC-INDEPENDENT PATHWAY, SUBSTRATES, AND DISRUPTION PHENOTYPE. RX PubMed=10949305; DOI=10.1038/35020586; RA Samuelson J.C., Chen M., Jiang F., Moeller I., Wiedmann M., Kuhn A., RA Phillips G.J., Dalbey R.E.; RT "YidC mediates membrane protein insertion in bacteria."; RL Nature 406:637-641(2000). RN [8] RP INTERACTION WITH FTSQ AFTER SECY, AND DISRUPTION PHENOTYPE. RX PubMed=11415986; DOI=10.1093/embo-reports/kve108; RA Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., RA Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.; RT "Sec-dependent membrane protein insertion: sequential interaction of RT nascent FtsQ with SecY and YidC."; RL EMBO Rep. 2:524-529(2001). RN [9] RP SRP- AND SEC-DEPENDENT INSERTION INTO MEMBRANES, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=11821429; DOI=10.1074/jbc.m200311200; RA Urbanus M.L., Froederberg L., Drew D., Bjoerk P., de Gier J.-W., RA Brunner J., Oudega B., Luirink J.; RT "Targeting, insertion, and localization of Escherichia coli YidC."; RL J. Biol. Chem. 277:12718-12723(2002). RN [10] RP INTERACTION WITH SECD AND SECF. RX PubMed=12068816; DOI=10.1046/j.1365-2958.2002.02972.x; RA Nouwen N., Driessen A.J.M.; RT "SecDFyajC forms a heterotetrameric complex with YidC."; RL Mol. Microbiol. 44:1397-1405(2002). RN [11] RP FUNCTION. RX PubMed=12724529; DOI=10.1073/pnas.0636761100; RA Van Der Laan M., Urbanus M.L., Ten Hagen-Jongman C.M., Nouwen N., RA Oudega B., Harms N., Driessen A.J.M., Luirink J.; RT "A conserved function of YidC in the biogenesis of respiratory chain RT complexes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5801-5806(2003). RN [12] RP MUTAGENESIS OF 23-TRP--LYS-27; 334-TRP--GLN-338; 483-PRO--THR-487 AND RP GLY-512. RX PubMed=12707259; DOI=10.1074/jbc.m301008200; RA Chen M., Xie K., Nouwen N., Driessen A.J., Dalbey R.E.; RT "Conditional lethal mutations separate the M13 procoat and Pf3 coat RT functions of YidC: different YidC structural requirements for membrane RT protein insertion."; RL J. Biol. Chem. 278:23295-23300(2003). RN [13] RP MUTAGENESIS OF ILE-361 AND LEU-436. RX PubMed=14506280; DOI=10.1074/jbc.m307362200; RA Jiang F., Chen M., Yi L., de Gier J.-W.L., Kuhn A., Dalbey R.E.; RT "Defining the regions of Escherichia coli YidC that contribute to RT activity."; RL J. Biol. Chem. 278:48965-48972(2003). RN [14] RP FUNCTION, AND ATP SYNTHASE SUBUNIT AND SECE AS SUBSTRATES. RX PubMed=12950181; DOI=10.1021/bi034309h; RA Yi L., Jiang F., Chen M., Cain B., Bolhuis A., Dalbey R.E.; RT "YidC is strictly required for membrane insertion of subunits a and c of RT the F(1)F(0)ATP synthase and SecE of the SecYEG translocase."; RL Biochemistry 42:10537-10544(2003). RN [15] RP FUNCTION IN TARGETING AND/OR TRANSLOCATION OF LIPOPROTEINS. RX PubMed=15140892; DOI=10.1074/jbc.m403229200; RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.; RT "Targeting and translocation of two lipoproteins in Escherichia coli via RT the SRP/Sec/YidC pathway."; RL J. Biol. Chem. 279:31026-31032(2004). RN [16] RP FUNCTION IN FOLDING BUT NOT INSERTION OF LACY, AND DISRUPTION PHENOTYPE. RX PubMed=15067017; DOI=10.1083/jcb.200402067; RA Nagamori S., Smirnova I.N., Kaback H.R.; RT "Role of YidC in folding of polytopic membrane proteins."; RL J. Cell Biol. 165:53-62(2004). RN [17] RP SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=BL21-DE3; RX PubMed=16079137; DOI=10.1074/jbc.m506479200; RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., RA von Heijne G., Daley D.O.; RT "Protein complexes of the Escherichia coli cell envelope."; RL J. Biol. Chem. 280:34409-34419(2005). RN [18] RP FUNCTION OF PERIPLASMIC DOMAIN. RX PubMed=17073462; DOI=10.1021/bi060826z; RA Xie K., Kiefer D., Nagler G., Dalbey R.E., Kuhn A.; RT "Different regions of the nonconserved large periplasmic domain of RT Escherichia coli YidC are involved in the SecF interaction and membrane RT insertase activity."; RL Biochemistry 45:13401-13408(2006). RN [19] RP INTERACTION WITH FTSH. RX PubMed=18387365; DOI=10.1016/j.febslet.2008.02.082; RA van Bloois E., Dekker H.L., Froderberg L., Houben E.N., Urbanus M.L., RA de Koster C.G., de Gier J.W., Luirink J.; RT "Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role RT for these proteins in quality control upon insertion of bacterial inner RT membrane proteins."; RL FEBS Lett. 582:1419-1424(2008). RN [20] RP COMPLEMENTATION BY AND IN STREPTOCOCCUS MUTANS. 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). RN [21] RP FUNCTION IN FOLDING BUT NOT INSERTION OF MALF OR OF MALFGK(2) COMPLEX. RX PubMed=18456666; DOI=10.1074/jbc.m801481200; RA Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M., RA Genevaux P., Luirink J., de Gier J.W.; RT "Biogenesis of MalF and the MalFGK(2) maltose transport complex in RT Escherichia coli requires YidC."; RL J. Biol. Chem. 283:17881-17890(2008). RN [22] RP COMPLEMENTATION BY SPOIIIJ AND YQJG OF B.SUBTILIS. RX PubMed=19717609; DOI=10.1128/jb.00853-09; RA Saller M.J., Fusetti F., Driessen A.J.; RT "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein RT biogenesis."; RL J. Bacteriol. 191:6749-6757(2009). RN [23] RP DISRUPTION PHENOTYPE. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=21778229; DOI=10.1074/jbc.m111.245696; RA Fontaine F., Fuchs R.T., Storz G.; RT "Membrane localization of small proteins in Escherichia coli."; RL J. Biol. Chem. 286:32464-32474(2011). RN [24] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=BL21-DE3; RX PubMed=27435098; DOI=10.1042/bcj20160545; RA Komar J., Alvira S., Schulze R.J., Martin R., Lycklama a Nijeholt J.A., RA Lee S.C., Dafforn T.R., Deckers-Hebestreit G., Berger I., Schaffitzel C., RA Collinson I.; RT "Membrane protein insertion and assembly by the bacterial holo-translocon RT SecYEG-SecDF-YajC-YidC."; RL Biochem. J. 473:3341-3354(2016). RN [25] {ECO:0007744|PDB:3BLC} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-340. RC STRAIN=K12; RX PubMed=18093969; DOI=10.1074/jbc.m708936200; RA Oliver D.C., Paetzel M.; RT "Crystal structure of the major periplasmic domain of the bacterial RT membrane protein assembly facilitator YidC."; RL J. Biol. Chem. 283:5208-5216(2008). RN [26] {ECO:0007744|PDB:3BS6} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 56-329. RX PubMed=18234665; DOI=10.1074/jbc.m710493200; RA Ravaud S., Stjepanovic G., Wild K., Sinning I.; RT "The crystal structure of the periplasmic domain of the Escherichia coli RT membrane protein insertase YidC contains a substrate binding cleft."; RL J. Biol. Chem. 283:9350-9358(2008). RN [27] RP REVIEW. RX PubMed=21275640; DOI=10.1146/annurev-biochem-060409-092524; RA Dalbey R.E., Wang P., Kuhn A.; RT "Assembly of bacterial inner membrane proteins."; RL Annu. Rev. Biochem. 80:161-187(2011). CC -!- FUNCTION: Inner membrane protein required for the insertion and/or CC proper folding and/or complex formation of integral inner membrane CC proteins. Involved in integration of membrane proteins that insert CC dependently and independently of the Sec translocase complex, as well CC as at least 2 lipoproteins. Its own insertion requires SRP and is Sec CC translocase-dependent. Essential for the integration of Sec-dependent CC subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec- CC independent subunit c of the F(0)ATP synthase, M13 phage procoat and CC the N-terminus of leader peptidase Lep. Probably interacts directly CC with Sec-independent substrates. Sec-dependent protein FtsQ interacts CC first with SecY then subsequently with YidC. Sec-dependent LacY and CC MalF require YidC to acquire tertiary structure and stability, a CC chaperone-like function, but not for membrane insertion. Stable maltose CC transport copmplex formation (MalFGK(2)) also requires YidC. Partially CC complements a Streptococcus mutans yidC2 disruption mutant. CC {ECO:0000269|PubMed:10675323, ECO:0000269|PubMed:10949305, CC ECO:0000269|PubMed:12724529, ECO:0000269|PubMed:12950181, CC ECO:0000269|PubMed:15067017, ECO:0000269|PubMed:15140892, CC ECO:0000269|PubMed:17073462, ECO:0000269|PubMed:18456666}. CC -!- SUBUNIT: Interacts with SecD and SecF. Component of the SecDF-YajC CC complex, a heterotetrameric translocase complex. The SecDF-YidC-YajC CC translocase forms a supercomplex with SecYEG, called the holo- CC translocon (HTL) (PubMed:27435098). The stoichiometry of the super CC complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted CC complex (with SecDF) but as no antibody is available it could not be CC quantified (PubMed:27435098). Specifically interacts with transmembrane CC segments of nascent integral membrane proteins during membrane CC integration. Found in 3 different complexes in inner membrane CC preparations (PubMed:16079137). Can be cross-linked to FtsH, in the CC larger FtsH/HflKC complex. {ECO:0000269|PubMed:10675323, CC ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:12068816, CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:18387365, CC ECO:0000269|PubMed:27435098}. CC -!- INTERACTION: CC P25714; P03623: VIII; Xeno; NbExp=5; IntAct=EBI-6400779, EBI-8482910; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11821429, CC ECO:0000269|PubMed:16079137}; Multi-pass membrane protein CC {ECO:0000269|PubMed:11821429, ECO:0000269|PubMed:16079137}. CC Note=Predominantly localized at cell poles at all stages of cell CC growth. CC -!- INDUCTION: At mid-exponential phase in strain MC4100 there are about CC 2500 copies per cell (at protein level). CC -!- DOMAIN: Most of the large periplasmic domain (residues 24-264) is not CC required for either Sec-dependent or Sec-independent protein insertion. CC However, residues 265-346, the C-terminal part of the large periplasmic CC domain, are required for both Sec-dependent and Sec-independent protein CC insertion. CC -!- DISRUPTION PHENOTYPE: Lethality. Upon depletion experiments insertion CC of Sec translocase-independent integral membrane proteins ceases. CC Translocation of Sec-dependent protein decreases to a lesser extent. CC Also leads to decreased targeting and/or translocation of Lpp and BRP CC lipoproteins. Both spoIIIJ and yqjG of B.subtilis functionally CC complement yidC depletion, whereas Streptococcus mutans yidC1 and yidC2 CC only partially complement depletion. {ECO:0000269|PubMed:10949305, CC ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:15067017, CC ECO:0000269|PubMed:21778229}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10328; AAA62056.1; -; Genomic_DNA. DR EMBL; U00096; AAC76728.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77588.1; -; Genomic_DNA. DR EMBL; M11056; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B65173; B65173. DR RefSeq; NP_418161.1; NC_000913.3. DR RefSeq; WP_000378250.1; NZ_SSZK01000035.1. DR PDB; 3BLC; X-ray; 2.50 A; A/B=26-340. DR PDB; 3BS6; X-ray; 1.80 A; A/B=56-329. DR PDB; 4UTQ; EM; 8.00 A; A=1-548. DR PDB; 5M5H; EM; 4.50 A; A=1-540. DR PDB; 5MG3; EM; 14.00 A; C=2-548. DR PDB; 6AL2; X-ray; 2.80 A; A/B=1-540. DR PDBsum; 3BLC; -. DR PDBsum; 3BS6; -. DR PDBsum; 4UTQ; -. DR PDBsum; 5M5H; -. DR PDBsum; 5MG3; -. DR PDBsum; 6AL2; -. DR AlphaFoldDB; P25714; -. DR EMDB; EMD-2705; -. DR EMDB; EMD-3506; -. DR SMR; P25714; -. DR BioGRID; 4261511; 290. DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex. DR DIP; DIP-12442N; -. DR IntAct; P25714; 31. DR MINT; P25714; -. DR STRING; 511145.b3705; -. DR TCDB; 2.A.9.3.1; the membrane protein insertase (yidc/alb3/oxa1) family. DR jPOST; P25714; -. DR PaxDb; 511145-b3705; -. DR DNASU; 948214; -. DR EnsemblBacteria; AAC76728; AAC76728; b3705. DR GeneID; 75173922; -. DR GeneID; 948214; -. DR KEGG; ecj:JW3683; -. DR KEGG; eco:b3705; -. DR PATRIC; fig|1411691.4.peg.2998; -. DR EchoBASE; EB1183; -. DR eggNOG; COG0706; Bacteria. DR HOGENOM; CLU_016535_3_0_6; -. DR InParanoid; P25714; -. DR OMA; YAEFGWV; -. DR OrthoDB; 9780552at2; -. DR PhylomeDB; P25714; -. DR BioCyc; EcoCyc:YIDC; -. DR BioCyc; MetaCyc:YIDC; -. DR EvolutionaryTrace; P25714; -. DR PRO; PR:P25714; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032977; F:membrane insertase activity; IDA:EcoCyc. DR GO; GO:0006457; P:protein folding; IMP:UniProtKB. DR GO; GO:0051205; P:protein insertion into membrane; IDA:EcoliWiki. DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:ComplexPortal. DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal. DR GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB. 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. DR PRINTS; PR01900; YIDCPROTEIN. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..548 FT /note="Membrane protein insertase YidC" FT /id="PRO_0000124712" FT TOPO_DOM 1..5 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 6..23 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 24..342 FT /note="Periplasmic" FT TRANSMEM 343..370 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 371..416 FT /note="Cytoplasmic" FT TRANSMEM 417..446 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 447..463 FT /note="Periplasmic" FT TRANSMEM 464..481 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 482..493 FT /note="Cytoplasmic" FT TRANSMEM 494..509 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 510..512 FT /note="Periplasmic" FT TRANSMEM 513..535 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 536..548 FT /note="Cytoplasmic" FT REGION 24..264 FT /note="Can be removed without causing lethality, FT dispensible for M13 procoat processing" FT REGION 28..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 215..265 FT /note="Interaction with SecF; not required for insertion of FT a number of Sec-dependent or Sec-independent substrates" FT REGION 265..346 FT /note="Required for Sec-dependent and Sec-independent FT protein insertion" FT REGION 527..548 FT /note="Can be removed without causing lethality, FT dispensible for M13 procoat processing" FT COMPBIAS 28..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 24..27 FT /note="EQDK->IEGR: Cold-sensitive at 30 degrees Celsius; FT when associated with 334-W--G-338. Protein accumulates FT stably." FT MUTAGEN 334..338 FT /note="WFISQ->LEVLFQG: Cold-sensitive at 30 degrees FT Celsius; when associated with 24-I--R-27. Protein FT accumulates stably." FT /evidence="ECO:0000269|PubMed:12707259" FT MUTAGEN 361 FT /note="I->S: Loss of function." FT /evidence="ECO:0000269|PubMed:14506280" FT MUTAGEN 436 FT /note="L->S: Loss of function." FT /evidence="ECO:0000269|PubMed:14506280" FT MUTAGEN 483..487 FT /note="PTTVT->LVPRGS: Temperature-sensitive at 42 degrees FT Celsius; when associated with 512-ENLYFQG. Protein is not FT stable." FT /evidence="ECO:0000269|PubMed:12707259" FT MUTAGEN 512 FT /note="G->ENLYFQG: Temperature-sensitive at 42 degrees FT Celsius; when associated with 483-L--S-487. Protein is not FT stable." FT /evidence="ECO:0000269|PubMed:12707259" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 78..90 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 95..103 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 106..116 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 136..139 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 145..154 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 160..168 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 173..181 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 188..201 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:6AL2" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:6AL2" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:3BS6" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 235..239 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 260..280 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:3BS6" FT STRAND 300..311 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 314..320 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 324..327 FT /evidence="ECO:0007829|PDB:3BS6" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 334..351 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 354..368 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 370..385 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 387..397 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 401..414 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 421..423 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 424..442 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 466..481 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 489..506 FT /evidence="ECO:0007829|PDB:6AL2" FT HELIX 511..531 FT /evidence="ECO:0007829|PDB:6AL2" SQ SEQUENCE 548 AA; 61526 MW; 95EBC5DAB4F2FCFB CRC64; MDSQRNLLVI ALLFVSFMIW QAWEQDKNPQ PQAQQTTQTT TTAAGSAADQ GVPASGQGKL ISVKTDVLDL TINTRGGDVE QALLPAYPKE LNSTQPFQLL ETSPQFIYQA QSGLTGRDGP DNPANGPRPL YNVEKDAYVL AEGQNELQVP MTYTDAAGNT FTKTFVLKRG DYAVNVNYNV QNAGEKPLEI SSFGQLKQSI TLPPHLDTGS SNFALHTFRG AAYSTPDEKY EKYKFDTIAD NENLNISSKG GWVAMLQQYF ATAWIPHNDG TNNFYTANLG NGIAAIGYKS QPVLVQPGQT GAMNSTLWVG PEIQDKMAAV APHLDLTVDY GWLWFISQPL FKLLKWIHSF VGNWGFSIII ITFIVRGIMY PLTKAQYTSM AKMRMLQPKI QAMRERLGDD KQRISQEMMA LYKAEKVNPL GGCFPLLIQM PIFLALYYML MGSVELRQAP FALWIHDLSA QDPYYILPIL MGVTMFFIQK MSPTTVTDPM QQKIMTFMPV IFTVFFLWFP SGLVLYYIVS NLVTIIQQQL IYRGLEKRGL HSREKKKS //