TBPB_NEIMB
ID TBPB_NEIMB Reviewed; 712 AA.
AC Q9K0V0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Transferrin-binding protein B {ECO:0000303|PubMed:22327295};
DE Short=TbpB {ECO:0000303|PubMed:22327295};
DE AltName: Full=Surface lipoprotein TbpB {ECO:0000303|PubMed:27572441};
DE AltName: Full=Transferrin-binding protein 2;
DE Short=TBP-2;
DE Flags: Precursor;
GN Name=tbpB {ECO:0000303|PubMed:22327295};
GN Synonyms=tbp2 {ECO:0000303|PubMed:10710307}; OrderedLocusNames=NMB0460;
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 SUBCELLULAR LOCATION.
RC STRAIN=MC58;
RX PubMed=27572441; DOI=10.1038/nmicrobiol.2016.9;
RA Hooda Y., Lai C.C., Judd A., Buckwalter C.M., Shin H.E., Gray-Owen S.D.,
RA Moraes T.F.;
RT "Slam is an outer membrane protein that is required for the surface display
RT of lipidated virulence factors in Neisseria.";
RL Nat. Microbiol. 1:16009-16009(2016).
RN [4] {ECO:0007744|PDB:3V8U}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-712, FUNCTION,
RP TRANSFERRIN-BINDING, DOMAIN, AND MUTAGENESIS OF GLN-218; PHE-220; GLN-225
RP AND PRO-226.
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. Involved in the initial capture of TF.
CC Helps select only those TF molecules that can be used as an iron source
CC and concentrates them on the cell surface, maintaining the iron-loaded
CC status of the TF C-terminal lobe until its delivery to TbpA.
CC {ECO:0000269|PubMed:22327295}.
CC -!- SUBUNIT: Binds only human holo-transferrin (TF), via the TF C-terminus.
CC Forms a large complex with TF and TbpA (PubMed:22327295). Interacts via
CC its C-terminal domain with Slam1 (By similarity).
CC {ECO:0000250|UniProtKB:Q06988, ECO:0000269|PubMed:22327295}.
CC -!- INTERACTION:
CC Q9K0V0; P02787: TF; Xeno; NbExp=2; IntAct=EBI-15968994, EBI-714319;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:27572441}; Lipid-anchor {ECO:0000305}. Cell surface
CC {ECO:0000269|PubMed:27572441}. Note=Requires Slam1 for surface
CC expression in E.coli. {ECO:0000269|PubMed:27572441}.
CC -!- DOMAIN: Has 2 lobes, each of which has an 8-strand beta barrel flanked
CC on their N-terminus by a 4-strand handle domain. Electron microscopy
CC suggests that in the TbpA-TbpB-TF complex, TF is captured directly
CC above the loop domain of TbpA in a chamber of about 1000 Angstroms(3)
CC formed by the 3 proteins, where interactions between the proteins serve
CC to abstract iron 2 from TF. {ECO:0000269|PubMed:22327295}.
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 TbpB family. Isotype II subfamily.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF40897.1; -; Genomic_DNA.
DR PIR; E81196; E81196.
DR RefSeq; NP_273507.1; NC_003112.2.
DR RefSeq; WP_010980796.1; NC_003112.2.
DR PDB; 3V8U; X-ray; 2.40 A; A/B=22-711.
DR PDBsum; 3V8U; -.
DR AlphaFoldDB; Q9K0V0; -.
DR SMR; Q9K0V0; -.
DR DIP; DIP-59654N; -.
DR IntAct; Q9K0V0; 2.
DR STRING; 122586.NMB0460; -.
DR PaxDb; Q9K0V0; -.
DR PRIDE; Q9K0V0; -.
DR EnsemblBacteria; AAF40897; AAF40897; NMB0460.
DR KEGG; nme:NMB0460; -.
DR PATRIC; fig|122586.8.peg.600; -.
DR HOGENOM; CLU_024250_0_0_4; -.
DR OMA; GWFAYPG; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0071281; P:cellular response to iron ion; EXP:CollecTF.
DR Gene3D; 2.40.128.240; -; 1.
DR Gene3D; 2.40.128.250; -; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR001677; TbpB_B_D.
DR InterPro; IPR035316; TbpB_C-lobe.
DR InterPro; IPR038197; TbpB_C-lobe_sf.
DR InterPro; IPR035313; TbpB_N-lobe.
DR InterPro; IPR038669; TbpB_N-lobe_sf.
DR Pfam; PF17484; TbpB_A; 1.
DR Pfam; PF01298; TbpB_B_D; 2.
DR Pfam; PF17483; TbpB_C; 1.
DR SUPFAM; SSF56925; SSF56925; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..712
FT /note="Transferrin-binding protein B"
FT /id="PRO_0000018193"
FT REGION 59..196
FT /note="N-terminal handle domain"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 78..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..367
FT /note="N-terminal beta barrel domain"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 223..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..555
FT /note="C-terminal handle domain"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 442..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..712
FT /note="C-terminal beta barrel domain"
FT /evidence="ECO:0000269|PubMed:22327295"
FT REGION 689..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT MUTAGEN 218
FT /note="Q->E: Decreased binding to human transferrin (TF)."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 220
FT /note="F->E: Decreased binding to TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 225
FT /note="Q->A: Significantly decreased binding to TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 225
FT /note="Q->E: No longer binds TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 226
FT /note="P->A: Wild-type binding to TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT MUTAGEN 226
FT /note="P->E,R,W: No longer binds TF."
FT /evidence="ECO:0000269|PubMed:22327295"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:3V8U"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3V8U"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 153..172
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 176..192
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 511..520
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 544..553
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 565..580
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 590..601
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 602..605
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 606..612
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 620..628
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 631..637
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:3V8U"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 674..682
FT /evidence="ECO:0007829|PDB:3V8U"
FT STRAND 697..707
FT /evidence="ECO:0007829|PDB:3V8U"
SQ SEQUENCE 712 AA; 77417 MW; 77EA248941E8EF0C CRC64;
MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVFSE KPQAQKDQGG
YGFAMRLKRR NWYPQAKEDE VKLDESDWEA TGLPDEPKEL PKRQKSVIEK VETDSDNNIY
SSPYLKPSNH QNGNTGNGIN QPKNQAKDYE NFKYVYSGWF YKHAKREFNL KVEPKSAKNG
DDGYIFYHGK EPSRQLPASG KITYKGVWHF ATDTKKGQKF REIIQPSKSQ GDRYSGFSGD
DGEEYSNKNK STLTDGQEGY GFTSNLEVDF HNKKLTGKLI RNNANTDNNQ ATTTQYYSLE
AQVTGNRFNG KATATDKPQQ NSETKEHPFV SDSSSLSGGF FGPQGEELGF RFLSDDQKVA
VVGSAKTKDK PANGNTAAAS GGTDAAASNG AAGTSSENGK LTTVLDAVEL KLGDKEVQKL
DNFSNAAQLV VDGIMIPLLP EASESGNNQA NQGTNGGTAF TRKFDHTPES DKKDAQAGTQ
TNGAQTASNT AGDTNGKTKT YEVEVCCSNL NYLKYGMLTR KNSKSAMQAG ESSSQADAKT
EQVEQSMFLQ GERTDEKEIP SEQNIVYRGS WYGYIANDKS TSWSGNASNA TSGNRAEFTV
NFADKKITGT LTADNRQEAT FTIDGNIKDN GFEGTAKTAE SGFDLDQSNT TRTPKAYITD
AKVQGGFYGP KAEELGGWFA YPGDKQTKNA TNASGNSSAT VVFGAKRQQP VR
