TOLB_ECOLI
ID TOLB_ECOLI Reviewed; 430 AA.
AC P0A855; P19935;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tol-Pal system protein TolB {ECO:0000255|HAMAP-Rule:MF_00671, ECO:0000305};
DE Flags: Precursor;
GN Name=tolB {ECO:0000255|HAMAP-Rule:MF_00671, ECO:0000303|PubMed:2687247};
GN OrderedLocusNames=b0740, JW5100;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / JM105 / ATCC 47016;
RX PubMed=2687247; DOI=10.1128/jb.171.12.6600-6609.1989;
RA Levengood S.K., Webster R.E.;
RT "Nucleotide sequences of the tolA and tolB genes and localization of their
RT products, components of a multistep translocation system in Escherichia
RT coli.";
RL J. Bacteriol. 171:6600-6609(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-430.
RC STRAIN=K12;
RX PubMed=1574003; DOI=10.1111/j.1365-2958.1992.tb01523.x;
RA Lazzaroni J.-C., Portalier R.;
RT "The excC gene of Escherichia coli K-12 required for cell envelope
RT integrity encodes the peptidoglycan-associated lipoprotein (PAL).";
RL Mol. Microbiol. 6:735-742(1992).
RN [6]
RP PROTEIN SEQUENCE OF 22-27, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7929011; DOI=10.1128/jb.176.20.6392-6396.1994;
RA Isnard M., Rigal A., Lazzaroni J.-C., Lazdunski C., Lloubes R.;
RT "Maturation and localization of the TolB protein required for colicin
RT import.";
RL J. Bacteriol. 176:6392-6396(1994).
RN [7]
RP PROTEIN SEQUENCE OF 22-32.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [8]
RP INTERACTION WITH PAL, AND SUBCELLULAR LOCATION.
RX PubMed=7744736; DOI=10.1074/jbc.270.19.11071;
RA Bouveret E., Derouiche R., Rigal A., Lloubes R., Lazdunski C.,
RA Benedetti H.;
RT "Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to
RT explaining the formation of contact sites between the inner and outer
RT membranes of Escherichia coli.";
RL J. Biol. Chem. 270:11071-11077(1995).
RN [9]
RP INTERACTION WITH PORINS.
RX PubMed=9393690; DOI=10.1128/jb.179.23.7274-7279.1997;
RA Rigal A., Bouveret E., Lloubes R., Lazdunski C., Benedetti H.;
RT "The TolB protein interacts with the porins of Escherichia coli.";
RL J. Bacteriol. 179:7274-7279(1997).
RN [10]
RP INTERACTION WITH PAL; LPP AND OMPA.
RX PubMed=9701827; DOI=10.1046/j.1365-2958.1998.00945.x;
RA Clavel T., Germon P., Vianney A., Portalier R., Lazzaroni J.-C.;
RT "TolB protein of Escherichia coli K-12 interacts with the outer membrane
RT peptidoglycan-associated proteins Pal, Lpp and OmpA.";
RL Mol. Microbiol. 29:359-367(1998).
RN [11]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH TOLA.
RX PubMed=11994151; DOI=10.1046/j.1365-2958.2002.02895.x;
RA Walburger A., Lazdunski C., Corda Y.;
RT "The Tol/Pal system function requires an interaction between the C-terminal
RT domain of TolA and the N-terminal domain of TolB.";
RL Mol. Microbiol. 44:695-708(2002).
RN [12]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17233825; DOI=10.1111/j.1365-2958.2006.05571.x;
RA Gerding M.A., Ogata Y., Pecora N.D., Niki H., de Boer P.A.;
RT "The trans-envelope Tol-Pal complex is part of the cell division machinery
RT and required for proper outer-membrane invagination during cell
RT constriction in E. coli.";
RL Mol. Microbiol. 63:1008-1025(2007).
RN [13]
RP FUNCTION.
RX PubMed=24720726; DOI=10.1111/mmi.12609;
RA Santos T.M., Lin T.Y., Rajendran M., Anderson S.M., Weibel D.B.;
RT "Polar localization of Escherichia coli chemoreceptors requires an intact
RT Tol-Pal complex.";
RL Mol. Microbiol. 92:985-1004(2014).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32152098; DOI=10.1073/pnas.1919267117;
RA Yakhnina A.A., Bernhardt T.G.;
RT "The Tol-Pal system is required for peptidoglycan-cleaving enzymes to
RT complete bacterial cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:6777-6783(2020).
RN [15]
RP CRYSTALLIZATION.
RX PubMed=9761825; DOI=10.1107/s0907444997008020;
RA Abergel C., Rigal A., Chenivesse S., Lazdunski C., Claverie J.-M.,
RA Bouveret E., Benedetti H.;
RT "Crystallization and preliminary crystallographic study of a component of
RT the Escherichia coli Tol system: TolB.";
RL Acta Crystallogr. D 54:102-104(1998).
RN [16] {ECO:0007744|PDB:1CRZ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=10545334; DOI=10.1016/s0969-2126(00)80062-3;
RA Abergel C., Bouveret E., Claverie J.-M., Brown K., Rigal A., Lazdunski C.,
RA Benedetti H.;
RT "Structure of the Escherichia coli TolB protein determined by MAD methods
RT at 1.95-A resolution.";
RL Structure 7:1291-1300(1999).
RN [17] {ECO:0007744|PDB:1C5K}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND INTERACTION WITH COLICIN E9.
RX PubMed=10673426; DOI=10.1016/s0969-2126(00)00079-4;
RA Carr S., Penfold C.N., Bamford V., James R., Hemmings A.M.;
RT "The structure of TolB, an essential component of the tol-dependent
RT translocation system, and its protein-protein interaction with the
RT translocation domain of colicin E9.";
RL Structure 8:57-66(2000).
RN [18] {ECO:0007744|PDB:2IVZ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COLICIN E9.
RX PubMed=16894158; DOI=10.1073/pnas.0603433103;
RA Loftus S.R., Walker D., Mate M.J., Bonsor D.A., James R., Moore G.R.,
RA Kleanthous C.;
RT "Competitive recruitment of the periplasmic translocation portal TolB by a
RT natively disordered domain of colicin E9.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12353-12358(2006).
RN [19] {ECO:0007744|PDB:2HQS}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 23-430 IN COMPLEX WITH PAL.
RX PubMed=17375930; DOI=10.1021/ja070153n;
RA Bonsor D.A., Grishkovskaya I., Dodson E.J., Kleanthous C.;
RT "Molecular mimicry enables competitive recruitment by a natively disordered
RT protein.";
RL J. Am. Chem. Soc. 129:4800-4807(2007).
RN [20] {ECO:0007744|PDB:2W8B}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 22-430 IN COMPLEX WITH PAL,
RP FUNCTION, AND DOMAIN.
RX PubMed=19696740; DOI=10.1038/emboj.2009.224;
RA Bonsor D.A., Hecht O., Vankemmelbeke M., Sharma A., Krachler A.M.,
RA Housden N.G., Lilly K.J., James R., Moore G.R., Kleanthous C.;
RT "Allosteric beta-propeller signalling in TolB and its manipulation by
RT translocating colicins.";
RL EMBO J. 28:2846-2857(2009).
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity (PubMed:17233825). TolB occupies a
CC key intermediary position in the Tol-Pal system because it communicates
CC directly with both membrane-embedded components, Pal in the outer
CC membrane and TolA in the inner membrane (PubMed:19696740). The Tol-Pal
CC system is also required for polar localization of chemoreceptors
CC clusters (PubMed:24720726). The system also appears to be required for
CC the activity of several outer membrane-localized enzymes with cell wall
CC remodeling activity (PubMed:32152098). Is involved in the uptake of
CC some colicins A (PubMed:2687247, PubMed:7929011, PubMed:11994151).
CC {ECO:0000269|PubMed:11994151, ECO:0000269|PubMed:17233825,
CC ECO:0000269|PubMed:19696740, ECO:0000269|PubMed:24720726,
CC ECO:0000269|PubMed:32152098, ECO:0000305|PubMed:2687247,
CC ECO:0000305|PubMed:7929011}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer
CC (PubMed:17233825). TolB forms homodimers (PubMed:11994151). Interacts
CC with the peptidoglycan-associated lipoprotein Pal and with the C-
CC terminal region of TolA (PubMed:7744736, PubMed:11994151,
CC PubMed:17375930, PubMed:19696740). Interacts with the trimeric porins
CC OmpF, OmpC, PhoE and LamB (PubMed:9393690). Can form a complex with
CC Pal, Lpp and OmpA (PubMed:9701827). Interacts with colicin E9
CC (PubMed:10673426, PubMed:16894158). {ECO:0000269|PubMed:10673426,
CC ECO:0000269|PubMed:11994151, ECO:0000269|PubMed:16894158,
CC ECO:0000269|PubMed:17375930, ECO:0000269|PubMed:19696740,
CC ECO:0000269|PubMed:7744736, ECO:0000269|PubMed:9393690,
CC ECO:0000269|PubMed:9701827, ECO:0000305|PubMed:17233825}.
CC -!- INTERACTION:
CC P0A855; P0A912: pal; NbExp=4; IntAct=EBI-7180728, EBI-1124760;
CC P0A855; P19934: tolA; NbExp=5; IntAct=EBI-7180728, EBI-1120026;
CC P0A855; P09883: col; Xeno; NbExp=9; IntAct=EBI-7180728, EBI-1029888;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00671,
CC ECO:0000269|PubMed:2687247, ECO:0000269|PubMed:7929011}. Note=Partially
CC associated with the outer membrane through a specific interaction with
CC Pal (PubMed:7744736). Accumulates at cell constriction sites.
CC Recruitment to the division site is dependent on FtsN activity
CC (PubMed:17233825). {ECO:0000269|PubMed:17233825,
CC ECO:0000269|PubMed:7744736}.
CC -!- DOMAIN: Effector proteins that bind to TolB can both negatively (Pal)
CC and positively (colicin E9) regulate association of the distal N-
CC terminal TolA box with TolA by influencing the conformational
CC equilibrium experienced by these residues.
CC {ECO:0000269|PubMed:19696740}.
CC -!- DISRUPTION PHENOTYPE: Mutants lacking the tol-pal cluster suffer
CC delayed outer membrane invagination and contain large outer membrane
CC blebs at constriction sites and cell poles (PubMed:17233825). Tol-pal
CC mutants fail to complete division and form cell chains, and fail to
CC process denuded peptidoglycans at the septum (PubMed:32152098).
CC {ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:32152098}.
CC -!- SIMILARITY: Belongs to the TolB family. {ECO:0000255|HAMAP-
CC Rule:MF_00671, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M28232; AAA24684.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73834.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35406.2; -; Genomic_DNA.
DR EMBL; X65796; CAA46672.1; -; Genomic_DNA.
DR PIR; C64810; C64810.
DR RefSeq; NP_415268.1; NC_000913.3.
DR RefSeq; WP_001295307.1; NZ_STEB01000035.1.
DR PDB; 1C5K; X-ray; 2.00 A; A=1-430.
DR PDB; 1CRZ; X-ray; 1.95 A; A=28-430.
DR PDB; 2HQS; X-ray; 1.50 A; A/B/D/F=23-430.
DR PDB; 2IVZ; X-ray; 2.00 A; A/B/C/D=1-430.
DR PDB; 2W8B; X-ray; 1.86 A; A/B/D/F=22-430.
DR PDB; 3IAX; X-ray; 2.60 A; A=1-430.
DR PDB; 7NST; EM; 3.70 A; E=1-430.
DR PDB; 7NSU; EM; 4.70 A; E=1-430.
DR PDBsum; 1C5K; -.
DR PDBsum; 1CRZ; -.
DR PDBsum; 2HQS; -.
DR PDBsum; 2IVZ; -.
DR PDBsum; 2W8B; -.
DR PDBsum; 3IAX; -.
DR PDBsum; 7NST; -.
DR PDBsum; 7NSU; -.
DR AlphaFoldDB; P0A855; -.
DR SMR; P0A855; -.
DR BioGRID; 4261828; 397.
DR BioGRID; 849803; 7.
DR ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR DIP; DIP-48262N; -.
DR IntAct; P0A855; 11.
DR MINT; P0A855; -.
DR STRING; 511145.b0740; -.
DR TCDB; 2.C.1.2.1; the tonb-exbb-exbd/tola-tolq-tolr outer membrane receptor energizers and stabilizers (tonb/tola) family.
DR SWISS-2DPAGE; P0A855; -.
DR jPOST; P0A855; -.
DR PaxDb; P0A855; -.
DR PRIDE; P0A855; -.
DR EnsemblBacteria; AAC73834; AAC73834; b0740.
DR EnsemblBacteria; BAA35406; BAA35406; BAA35406.
DR GeneID; 66670990; -.
DR GeneID; 945429; -.
DR KEGG; ecj:JW5100; -.
DR KEGG; eco:b0740; -.
DR PATRIC; fig|1411691.4.peg.1532; -.
DR EchoBASE; EB1001; -.
DR eggNOG; COG0823; Bacteria.
DR HOGENOM; CLU_047123_0_0_6; -.
DR InParanoid; P0A855; -.
DR OMA; VREPSWG; -.
DR PhylomeDB; P0A855; -.
DR BioCyc; EcoCyc:EG11008-MON; -.
DR BioCyc; MetaCyc:EG11008-MON; -.
DR EvolutionaryTrace; P0A855; -.
DR PRO; PR:P0A855; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
DR GO; GO:0043213; P:bacteriocin transport; IMP:EcoliWiki.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR GO; GO:0071237; P:cellular response to bacteriocin; IDA:EcoCyc.
DR GO; GO:0017038; P:protein import; IMP:EcoliWiki.
DR GO; GO:0015031; P:protein transport; IMP:EcoliWiki.
DR GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR Gene3D; 2.120.10.30; -; 1.
DR HAMAP; MF_00671; TolB; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR014167; Tol-Pal_TolB.
DR InterPro; IPR007195; TolB_N.
DR Pfam; PF07676; PD40; 4.
DR Pfam; PF04052; TolB_N; 1.
DR TIGRFAMs; TIGR02800; propeller_TolB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Direct protein sequencing;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00671,
FT ECO:0000269|PubMed:7929011, ECO:0000269|Ref.7"
FT CHAIN 22..430
FT /note="Tol-Pal system protein TolB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00671"
FT /id="PRO_0000034647"
FT REGION 22..34
FT /note="TolA box"
FT /evidence="ECO:0000305|PubMed:19696740"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1CRZ"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2HQS"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2HQS"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:2HQS"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1CRZ"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:2HQS"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:2HQS"
SQ SEQUENCE 430 AA; 45956 MW; 508795C6E6886B52 CRC64;
MKQALRVAFG FLILWASVLH AEVRIVIDSG VDSGRPIGVV PFQWAGPGAA PEDIGGIVAA
DLRNSGKFNP LDRARLPQQP GSAQEVQPAA WSALGIDAVV VGQVTPNPDG SYNVAYQLVD
TGGAPGTVLA QNSYKVNKQW LRYAGHTASD EVFEKLTGIK GAFRTRIAYV VQTNGGQFPY
ELRVSDYDGY NQFVVHRSPQ PLMSPAWSPD GSKLAYVTFE SGRSALVIQT LANGAVRQVA
SFPRHNGAPA FSPDGSKLAF ALSKTGSLNL YVMDLASGQI RQVTDGRSNN TEPTWFPDSQ
NLAFTSDQAG RPQVYKVNIN GGAPQRITWE GSQNQDADVS SDGKFMVMVS SNGGQQHIAK
QDLATGGVQV LSSTFLDETP SLAPNGTMVI YSSSQGMGSV LNLVSTDGRF KARLPATDGQ
VKFPAWSPYL
