TBPA_NEIMB
ID TBPA_NEIMB Reviewed; 915 AA.
AC Q9K0U9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transferrin-binding protein A {ECO:0000303|PubMed:22327295};
DE Short=TbpA {ECO:0000303|PubMed:22327295};
DE AltName: Full=Transferrin-binding protein 1 {ECO:0000303|PubMed:10710307};
DE Flags: Precursor;
GN Name=tbp1 {ECO:0000303|PubMed:10710307};
GN Synonyms=tbpA {ECO:0000303|PubMed:22327295}; OrderedLocusNames=NMB0461;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP HOST-SPECIFICITY.
RX PubMed=2110858; DOI=10.1139/m90-026;
RA Schryvers A.B., Gonzalez G.C.;
RT "Receptors for transferrin in pathogenic bacteria are specific for the
RT host's protein.";
RL Can. J. Microbiol. 36:145-147(1990).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
RN [4] {ECO:0007744|PDB:3V89, ECO:0007744|PDB:3V8X}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-915 IN COMPLEX WITH HUMAN
RP TRANSFERRIN, FUNCTION, TRANSFERRIN-BINDING, SUBUNIT, DOMAIN, TOPOLOGY, AND
RP MUTAGENESIS OF ASP-251; 351-LYS--ALA-361; LYS-358; LYS-467; ASP-722 AND
RP ARG-825.
RC STRAIN=K454 / Serogroup B;
RX PubMed=22327295; DOI=10.1038/nature10823;
RA Noinaj N., Easley N.C., Oke M., Mizuno N., Gumbart J., Boura E.,
RA Steere A.N., Zak O., Aisen P., Tajkhorshid E., Evans R.W., Gorringe A.R.,
RA Mason A.B., Steven A.C., Buchanan S.K.;
RT "Structural basis for iron piracy by pathogenic Neisseria.";
RL Nature 483:53-58(2012).
CC -!- FUNCTION: Neisseria acquires iron by extracting it from serum
CC transferrin (TF) in its human host. Acts as a TF receptor and is
CC required for TF utilization. Binds both apo- and holo-TF, via the TF C-
CC terminus. {ECO:0000269|PubMed:22327295}.
CC -!- SUBUNIT: Binds both human apo- and holo-transferrin (TF), via the TF C-
CC terminus. Forms a large complex with TF and TbpB.
CC {ECO:0000269|PubMed:22327295}.
CC -!- INTERACTION:
CC Q9K0U9; P02787: TF; Xeno; NbExp=4; IntAct=EBI-15968954, EBI-714319;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:22327295}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:22327295}.
CC -!- DOMAIN: The N-terminal periplasmic domain encodes a plug that inserts
CC into the 22 beta-strand barrel, the extracellular loops extend up to 60
CC Angstroms away from the outer membrane. Part of the plug (the plug
CC loop, resides 121-139) interacts with transferrin (TF), as does the L3
CC helix finger in extracellular loop 3 (residues 351-361). When the L3
CC helix finger inserts into TF it disturbs the conformation of TF and its
CC coordination of iron 2. Electron microscopy suggests that in the TbpA-
CC TbpB-TF complex, TF is captured directly above the loop domain of TbpA
CC in a chamber of about 1000 Angstroms(3) formed by the 3 proteins, where
CC interactions between the proteins serve to abstract iron 2 from TF.
CC {ECO:0000269|PubMed:22327295}.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human. {ECO:0000269|PubMed:16645985}.
CC -!- MISCELLANEOUS: N.meningitidis cells will only bind to human TF, not
CC bovine or porcine TF, explaining at least in part the bacteria's
CC inability to cause infection in non-human hosts.
CC {ECO:0000269|PubMed:2110858}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF40898.1; -; Genomic_DNA.
DR PIR; F81196; F81196.
DR RefSeq; NP_273508.1; NC_003112.2.
DR RefSeq; WP_010980797.1; NC_003112.2.
DR PDB; 3V89; X-ray; 3.10 A; A=25-915.
DR PDB; 3V8X; X-ray; 2.60 A; A=25-915.
DR PDBsum; 3V89; -.
DR PDBsum; 3V8X; -.
DR AlphaFoldDB; Q9K0U9; -.
DR SMR; Q9K0U9; -.
DR DIP; DIP-59653N; -.
DR IntAct; Q9K0U9; 2.
DR STRING; 122586.NMB0461; -.
DR PaxDb; Q9K0U9; -.
DR EnsemblBacteria; AAF40898; AAF40898; NMB0461.
DR KEGG; nme:NMB0461; -.
DR PATRIC; fig|122586.8.peg.601; -.
DR HOGENOM; CLU_008287_19_0_4; -.
DR OMA; PSFAEMY; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IBA:GO_Central.
DR GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071702; P:organic substance transport; IEA:UniProt.
DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR039426; BtuB-like.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt.
DR InterPro; IPR010948; TonB_lacto/transferrin_rcpt.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR PANTHER; PTHR30069; PTHR30069; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1.
DR TIGRFAMs; TIGR01776; TonB-tbp-lbp; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Receptor; Reference proteome;
KW Signal; TonB box; Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..915
FT /note="Transferrin-binding protein A"
FT /id="PRO_0000349889"
FT TOPO_DOM 25..187
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 188..197
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 198..203
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 204..213
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 214..215
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 216..225
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 226..309
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 310..319
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 320..324
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 325..334
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 335..406
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 407..415
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 416..423
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 424..433
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 434..478
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 479..488
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 489..494
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 495..504
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 505..583
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 584..592
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 593..594
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 595..603
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 604..623
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 624..633
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 634..637
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 638..647
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 648..675
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 676..685
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 686..689
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 690..699
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 700..733
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 734..743
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 744..755
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 756..765
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 766..790
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 791..799
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 800..802
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 803..811
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 812..845
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 846..855
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 856..860
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 861..870
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TOPO_DOM 871..905
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22327295"
FT TRANSMEM 906..915
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 54..176
FT /note="Plug domain"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 121..139
FT /note="Plug loop, interacts with transferrin"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 351..361
FT /note="L3 helix finger, interacts with transferrin"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..45
FT /note="TonB box"
FT MOTIF 898..915
FT /note="TonB C-terminal box"
FT MUTAGEN 251
FT /note="D->A: Nearly complete loss of binding to human
FT transferrin (TF)."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 351..361
FT /note="Missing: No longer binds TF, changes surface protein
FT conformation."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 358
FT /note="K->A: Wild-type TF binding."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 467
FT /note="K->A: Binds about 50% TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 722
FT /note="D->A: Binds about 50% TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 825
FT /note="R->A: Binds about 75% TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3V8X"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 202..213
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 216..228
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3V89"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:3V8X"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3V8X"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 325..341
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:3V8X"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 393..415
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 424..450
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 465..488
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 494..527
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 547..560
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 575..592
FT /evidence="ECO:0007829|PDB:3V8X"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 596..610
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:3V89"
FT STRAND 620..632
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 635..649
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 653..657
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 673..686
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 689..742
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 756..771
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 775..779
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 790..798
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 802..813
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 818..821
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 822..826
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 832..837
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 845..856
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 859..870
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 877..880
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:3V8X"
FT HELIX 897..900
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 905..915
FT /evidence="ECO:0007829|PDB:3V8X"
SQ SEQUENCE 915 AA; 102107 MW; 110A3F38A59287D5 CRC64;
MQQQHLFRFN ILCLSLMTAL PAYAENVQAG QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK
LVKSSDTLSK EQVLNIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVS LTVDGVSQIQ
SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSV EQGSGALAGS VAFQTKTADD
VIGEGRQWGI QSKTAYSGKN RGLTQSIALA GRIGGAEALL IHTGRRAGEI RAHEDAGRGV
QSFNRLVPVE DSSNYAYFIV KEECKNGSYE TCKANPKKDV VGKDERQTVS TRDYTGPNRF
LADPLSYESR SWLFRPGFRF ENKRHYIGGI LEHTQQTFDT RDMTVPAFLT KAVFDANKKQ
AGSLPGNGKY AGNHKYGGLF TNGENGALVG AEYGTGVFYD ETHTKSRYGL EYVYTNADKD
TWADYARLSY DRQGIGLDNH FQQTHCSADG SDKYCRPSAD KPFSYYKSDR VIYGESHRLL
QAAFKKSFDT AKIRHNLSVN LGFDRFGSNL RHQDYYYQHA NRAYSSNTPP QNNGKKISPN
GSETSPYWVT IGRGNVVTGQ ICRLGNNTYT DCTPRSINGK SYYAAVRDNV RLGRWADVGA
GLRYDYRSTH SDDGSVSTGT HRTLSWNAGI VLKPTDWLDL TYRTSTGFRL PSFAEMYGWR
AGVQSKAVKI DPEKSFNKEA GIVFKGDFGN LEASWFNNAY RDLIVRGYEA QIKDGKEEAK
GDPAYLNAQS ARITGINILG KIDWNGVWDK LPEGWYSTFA YNRVRVRDIK KRADRTDIQS
HLFDAIQPSR YVVGLGYDQP EGKWGVNGML TYSKAKEITE LLGSRALLNG NSRNTKATAR
RTRPWYIVDV SGYYTVKKHF TLRAGVYNLL NYRYVTWENV RQTAGGAVNQ HKNVGVYNRY
AAPGRNYTFS LEMKF
