LPTD_ECOLI
ID LPTD_ECOLI Reviewed; 784 AA.
AC P31554; P75631;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411};
DE AltName: Full=Organic solvent tolerance protein;
DE Flags: Precursor;
GN Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA, yabG;
GN OrderedLocusNames=b0054, JW0053;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abe S., Okutsu T., Negishi T., Nakajima H., Aono R.;
RT "N-hexane sensitivity of Escherichia coli due to low expression of ostA/imp
RT by insertion of IS2 and identification of the gene product as an outer
RT membrane protein.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 25-29.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 25-32, SUBCELLULAR LOCATION, AND FUNCTION IN HEXANE
RP RESISTANCE.
RC STRAIN=K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220;
RX PubMed=12724388; DOI=10.1099/mic.0.25927-0;
RA Abe S., Okutsu T., Nakajima H., Kakuda N., Ohtsu I., Aono R.;
RT "N-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA
RT encoding an 87 kDa minor protein associated with the outer membrane.";
RL Microbiology 149:1265-1273(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2547691; DOI=10.1093/genetics/122.3.491;
RA Sampson B.A., Misra R., Benson S.A.;
RT "Identification and characterization of a new gene of Escherichia coli K-12
RT involved in outer membrane permeability.";
RL Genetics 122:491-501(1989).
RN [8]
RP FUNCTION IN HEXANE RESISTANCE.
RC STRAIN=K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220;
RX PubMed=7811102; DOI=10.1128/aem.60.12.4624-4626.1994;
RA Aono R., Negishi T., Nakajima H.;
RT "Cloning of organic solvent tolerance gene ostA that determines n-hexane
RT tolerance level in Escherichia coli.";
RL Appl. Environ. Microbiol. 60:4624-4626(1994).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DISULFIDE BONDS.
RX PubMed=12207697; DOI=10.1046/j.1365-2958.2002.03091.x;
RA Braun M., Silhavy T.J.;
RT "Imp/OstA is required for cell envelope biogenesis in Escherichia coli.";
RL Mol. Microbiol. 45:1289-1302(2002).
RN [10]
RP INDUCTION.
RX PubMed=14981317; DOI=10.1271/bbb.68.458;
RA Ohtsu I., Kakuda N., Tsukagoshi N., Dokyu N., Takagi H., Wachi M., Aono R.;
RT "Transcriptional analysis of the ostA/imp gene involved in organic solvent
RT sensitivity in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 68:458-461(2004).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH LPTE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16861298; DOI=10.1073/pnas.0604744103;
RA Wu T., McCandlish A.C., Gronenberg L.S., Chng S.-S., Silhavy T.J.,
RA Kahne D.;
RT "Identification of a protein complex that assembles lipopolysaccharide in
RT the outer membrane of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11754-11759(2006).
RN [13]
RP FUNCTION, AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=18424520; DOI=10.1128/jb.00270-08;
RA Sperandeo P., Lau F.K., Carpentieri A., De Castro C., Molinaro A., Deho G.,
RA Silhavy T.J., Polissi A.;
RT "Functional analysis of the protein machinery required for transport of
RT lipopolysaccharide to the outer membrane of Escherichia coli.";
RL J. Bacteriol. 190:4460-4469(2008).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=20446753; DOI=10.1021/bi100493e;
RA Chng S.S., Gronenberg L.S., Kahne D.;
RT "Proteins required for lipopolysaccharide assembly in Escherichia coli form
RT a transenvelope complex.";
RL Biochemistry 49:4565-4567(2010).
RN [15]
RP DISULFIDE BONDS, AND ASSEMBLY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20615876; DOI=10.1074/jbc.m110.119321;
RA Denoncin K., Vertommen D., Paek E., Collet J.F.;
RT "The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the
RT assembly of the essential beta-barrel protein LptD.";
RL J. Biol. Chem. 285:29425-29433(2010).
RN [16]
RP FUNCTION.
RX PubMed=21339611; DOI=10.1088/0953-8984/22/45/454124;
RA Haarmann R., Ibrahim M., Stevanovic M., Bredemeier R., Schleiff E.;
RT "The properties of the outer membrane localized Lipid A transporter LptD.";
RL J. Phys. Condens. Matter. 22:454124-454124(2010).
RN [17]
RP FUNCTION, INTERACTION WITH LPTE, AND DOMAIN.
RX PubMed=20203010; DOI=10.1073/pnas.0912872107;
RA Chng S.S., Ruiz N., Chimalakonda G., Silhavy T.J., Kahne D.;
RT "Characterization of the two-protein complex in Escherichia coli
RT responsible for lipopolysaccharide assembly at the outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5363-5368(2010).
RN [18]
RP DISULFIDE BONDS.
RX PubMed=20566849; DOI=10.1073/pnas.1007319107;
RA Ruiz N., Chng S.S., Hiniker A., Kahne D., Silhavy T.J.;
RT "Nonconsecutive disulfide bond formation in an essential integral outer
RT membrane protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12245-12250(2010).
RN [19]
RP INTERACTION WITH LPTE, DOMAIN, AND MUTAGENESIS OF 529-ASP--SER-538.
RX PubMed=21257904; DOI=10.1073/pnas.1015617108;
RA Freinkman E., Chng S.S., Kahne D.;
RT "The complex that inserts lipopolysaccharide into the bacterial outer
RT membrane forms a two-protein plug-and-barrel.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2486-2491(2011).
RN [20]
RP INTERACTION WITH LPTE.
RX PubMed=21257909; DOI=10.1073/pnas.1019089108;
RA Chimalakonda G., Ruiz N., Chng S.S., Garner R.A., Kahne D., Silhavy T.J.;
RT "Lipoprotein LptE is required for the assembly of LptD by the beta-barrel
RT assembly machine in the outer membrane of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2492-2497(2011).
RN [21]
RP INTERACTION WITH LPTA, AND DOMAIN.
RX PubMed=22668317; DOI=10.1021/bi300592c;
RA Freinkman E., Okuda S., Ruiz N., Kahne D.;
RT "Regulated assembly of the transenvelope protein complex required for
RT lipopolysaccharide export.";
RL Biochemistry 51:4800-4806(2012).
RN [22]
RP DISULFIDE BONDS.
RX PubMed=22936569; DOI=10.1126/science.1227215;
RA Chng S.S., Xue M., Garner R.A., Kadokura H., Boyd D., Beckwith J.,
RA Kahne D.;
RT "Disulfide rearrangement triggered by translocon assembly controls
RT lipopolysaccharide export.";
RL Science 337:1665-1668(2012).
RN [23]
RP ASSEMBLY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=23772069; DOI=10.1128/jb.00431-13;
RA Schwalm J., Mahoney T.F., Soltes G.R., Silhavy T.J.;
RT "Role for Skp in LptD assembly in Escherichia coli.";
RL J. Bacteriol. 195:3734-3742(2013).
RN [24]
RP ASSEMBLY.
RC STRAIN=K12;
RX PubMed=24003122; DOI=10.1073/pnas.1312012110;
RA Narita S., Masui C., Suzuki T., Dohmae N., Akiyama Y.;
RT "Protease homolog BepA (YfgC) promotes assembly and degradation of beta-
RT barrel membrane proteins in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3612-E3621(2013).
RN [25]
RP DEGRADATION BY DEGP; BEPA AND YCAL.
RX PubMed=28784813; DOI=10.1128/jb.00418-17;
RA Soltes G.R., Martin N.R., Park E., Sutterlin H.A., Silhavy T.J.;
RT "Distinctive roles for periplasmic proteases in the maintenance of
RT essential outer membrane protein assembly.";
RL J. Bacteriol. 199:E00418-E00418(2017).
CC -!- FUNCTION: Together with LptE, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane.
CC Contributes to n-hexane resistance. {ECO:0000255|HAMAP-Rule:MF_01411,
CC ECO:0000269|PubMed:12207697, ECO:0000269|PubMed:12724388,
CC ECO:0000269|PubMed:16861298, ECO:0000269|PubMed:18424520,
CC ECO:0000269|PubMed:20203010, ECO:0000269|PubMed:21339611,
CC ECO:0000269|PubMed:2547691, ECO:0000269|PubMed:7811102}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptE and LptA. May interact with LptE during
CC assembly of LptD by the beta-barrel assembly machine.
CC {ECO:0000255|HAMAP-Rule:MF_01411, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:16861298, ECO:0000269|PubMed:20203010,
CC ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:21257909,
CC ECO:0000269|PubMed:22668317}.
CC -!- INTERACTION:
CC P31554; P0ADV1: lptA; NbExp=4; IntAct=EBI-549369, EBI-1132001;
CC P31554; P0ADC1: lptE; NbExp=19; IntAct=EBI-549369, EBI-1119442;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01411, ECO:0000269|PubMed:12207697,
CC ECO:0000269|PubMed:12724388, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:20446753}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:14981317}.
CC -!- DOMAIN: Contains an N-terminal soluble domain that is likely
CC periplasmic and interacts with LptA, and a C-terminal transmembrane
CC domain, which is predicted to be a beta-barrel and interacts with LptE.
CC Residues 529-538 play a key role in interaction with LptE.
CC {ECO:0000269|PubMed:20203010, ECO:0000269|PubMed:21257904,
CC ECO:0000269|PubMed:22668317}.
CC -!- PTM: Contains two intramolecular disulfide bonds. At least one
CC disulfide bond is required for activity, and protein is probably fully
CC oxidized in vivo.
CC -!- DISRUPTION PHENOTYPE: Mutations alter the permeability of the outer
CC membrane resulting in increased sensitivity to detergents, antibiotics
CC and dyes. Depletion leads to filamentation followed by membrane rupture
CC and cell lysis. {ECO:0000269|PubMed:12207697,
CC ECO:0000269|PubMed:2547691}.
CC -!- MISCELLANEOUS: The correct assembly of LptD depends on the
CC thiol:disulfide interchange proteins DsbA and DsbC, the chaperone
CC proteins SurA and Skp, LptE and the chaperone/protease BepA
CC (PubMed:20566849, PubMed:20615876, PubMed:21257904, PubMed:21257909,
CC PubMed:23772069, PubMed:24003122). Incorrectly folded LptD can be
CC degraded by three different proteases, DegP, BepA and YcaL. These
CC proteases act at distinct points in the outer membrane protein assembly
CC (PubMed:24003122, PubMed:28784813). {ECO:0000269|PubMed:20566849,
CC ECO:0000269|PubMed:20615876, ECO:0000269|PubMed:21257904,
CC ECO:0000269|PubMed:21257909, ECO:0000269|PubMed:23772069,
CC ECO:0000269|PubMed:24003122, ECO:0000269|PubMed:28784813}.
CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP-
CC Rule:MF_01411}.
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DR EMBL; AB013134; BAA34130.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73165.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96622.1; -; Genomic_DNA.
DR PIR; F64726; F64726.
DR RefSeq; NP_414596.1; NC_000913.3.
DR RefSeq; WP_000746151.1; NZ_LN832404.1.
DR PDB; 4RHB; X-ray; 3.35 A; A/C=203-784.
DR PDBsum; 4RHB; -.
DR AlphaFoldDB; P31554; -.
DR SMR; P31554; -.
DR BioGRID; 4259723; 266.
DR ComplexPortal; CPX-1093; LptDE outer membrane translocon complex.
DR DIP; DIP-10029N; -.
DR IntAct; P31554; 8.
DR STRING; 511145.b0054; -.
DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family.
DR CarbonylDB; P31554; -.
DR SWISS-2DPAGE; P31554; -.
DR jPOST; P31554; -.
DR PaxDb; P31554; -.
DR PRIDE; P31554; -.
DR EnsemblBacteria; AAC73165; AAC73165; b0054.
DR EnsemblBacteria; BAB96622; BAB96622; BAB96622.
DR GeneID; 66671656; -.
DR GeneID; 945011; -.
DR KEGG; ecj:JW0053; -.
DR KEGG; eco:b0054; -.
DR PATRIC; fig|1411691.4.peg.2229; -.
DR EchoBASE; EB1529; -.
DR eggNOG; COG1452; Bacteria.
DR HOGENOM; CLU_009039_2_0_6; -.
DR InParanoid; P31554; -.
DR OMA; DYSHLDW; -.
DR PhylomeDB; P31554; -.
DR BioCyc; EcoCyc:EG11569-MON; -.
DR BioCyc; MetaCyc:EG11569-MON; -.
DR PRO; PR:P31554; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:1990351; C:transporter complex; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IMP:EcoCyc.
DR GO; GO:0015920; P:lipopolysaccharide transport; IC:ComplexPortal.
DR GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR InterPro; IPR020889; LipoPS_assembly_LptD.
DR InterPro; IPR007543; LptD_C.
DR InterPro; IPR005653; OstA-like_N.
DR Pfam; PF04453; LptD; 1.
DR Pfam; PF03968; LptD_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Disulfide bond; Membrane; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01411,
FT ECO:0000269|PubMed:12724388, ECO:0000269|PubMed:9298646"
FT CHAIN 25..784
FT /note="LPS-assembly protein LptD"
FT /id="PRO_0000020276"
FT DISULFID 31..724
FT DISULFID 173..725
FT MUTAGEN 529..538
FT /note="Missing: Impairs assembly of the LptD/LptE complex.
FT Does not form native disulfide bonds. Severely compromises
FT outer membrane integrity."
FT /evidence="ECO:0000269|PubMed:21257904"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 310..321
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 325..336
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 353..365
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 368..379
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 388..403
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 406..421
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 426..441
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 443..453
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 463..469
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 483..491
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 505..516
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 556..567
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 575..586
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 603..614
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 617..629
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 630..633
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 634..659
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 661..667
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 682..691
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 707..710
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 711..720
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 729..740
FT /evidence="ECO:0007829|PDB:4RHB"
FT TURN 741..744
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 745..755
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:4RHB"
FT HELIX 769..773
FT /evidence="ECO:0007829|PDB:4RHB"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:4RHB"
SQ SEQUENCE 784 AA; 89671 MW; 906EA3FE8F8D3E1E CRC64;
MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL PVTINADHAK
GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP VRTVDALGNV HYDDNQVILK
GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILDNGSF TSCLPGSDTW
SVVGSEIIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY
FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED
EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS TDGYATQKFS
VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ NDVGPFDTRI YGQAVHFVNT
RDDMPEATRV HLEPTINLPL SNNWGSINTE AKLLATHYQQ TNLDWYNSRN TTKLDESVNR
VMPQFKVDGK MVFERDMEML APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL
FRDRTYGGLD RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND
DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR LVQLNYRYAS
PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV GAYYYDTNAN KQADSMLGVQ
YSSCCYAIRV GYERKLNGWD NDKQHAVYDN AIGFNIELRG LSSNYGLGTQ EMLRSNILPY
QNTL
