TBPB2_NEIMI
ID TBPB2_NEIMI Reviewed; 599 AA.
AC Q06988;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Transferrin-binding protein B {ECO:0000305};
DE Short=TbpB {ECO:0000305};
DE AltName: Full=Surface lipoprotein TbpB {ECO:0000303|PubMed:27572441};
DE AltName: Full=Transferrin-binding protein 2 {ECO:0000303|PubMed:8344530};
DE Short=TBP-2;
DE Flags: Precursor;
GN Name=tbpB; Synonyms=tbp2 {ECO:0000303|PubMed:8344530};
OS Neisseria meningitidis serogroup B.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-34; 51-61;
RP 158-174; 279-283; 351-368 AND 564-585, TRANSFERRIN-BINDING, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
RX PubMed=8344530; DOI=10.1016/0378-1119(93)90348-7;
RA Legrain M., Mazarin V., Irwin S.W., Bouchon B., Quentin-Millet M.-J.,
RA Jacobs E., Schryvers A.B.;
RT "Cloning and characterization of Neisseria meningitidis genes encoding the
RT transferrin-binding proteins Tbp1 and Tbp2.";
RL Gene 130:73-80(1993).
RN [2]
RP PROTEIN SEQUENCE OF 21-39.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
RX PubMed=8319886; DOI=10.1111/j.1574-6968.1993.tb06148.x;
RA Griffiths E., Stevenson P., Byfield P., Ala'Aldeen D.A.A., Borriello S.P.,
RA Holland J., Parsons T., Williams P.;
RT "Antigenic relationships of transferrin-binding proteins from Neisseria
RT meningitidis, N. gonorrhoeae and Haemophilus influenzae: cross-reactivity
RT of antibodies to NH2-terminal peptides.";
RL FEMS Microbiol. Lett. 109:85-91(1993).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
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 [5] {ECO:0007744|PDB:4QQ1}
RP X-RAY CRYSTALLOGRAPHY (3.33 ANGSTROMS) OF 58-599, AND DOMAIN.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
RX PubMed=25800619; DOI=10.1002/mbo3.254;
RA Adamiak P., Calmettes C., Moraes T.F., Schryvers A.B.;
RT "Patterns of structural and sequence variation within isotype lineages of
RT the Neisseria meningitidis transferrin receptor system.";
RL MicrobiologyOpen 4:491-504(2015).
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:0000250|UniProtKB:Q09057, ECO:0000305|PubMed:25800619,
CC ECO:0000305|PubMed:8344530}.
CC -!- SUBUNIT: Binds only human holo-transferrin (TF), via the TF C-terminus.
CC Forms a large complex with TF and TbpA (By similarity). Interacts via
CC its C-terminal domain with Slam1 (PubMed:27572441).
CC {ECO:0000250|UniProtKB:Q9K0V0, ECO:0000269|PubMed:27572441}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:27572441,
CC ECO:0000305|PubMed:8344530}; Lipid-anchor {ECO:0000305|PubMed:8344530}.
CC Cell surface {ECO:0000269|PubMed:27572441, ECO:0000269|PubMed:8344530}.
CC -!- INDUCTION: By iron starvation.
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.
CC {ECO:0000269|PubMed:25800619}.
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 I subfamily.
CC {ECO:0000305|PubMed:25800619}.
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DR EMBL; Z15129; CAA78830.1; -; Genomic_DNA.
DR PIR; JN0818; JN0818.
DR PDB; 4QQ1; X-ray; 3.33 A; A/B/C=58-599.
DR PDBsum; 4QQ1; -.
DR AlphaFoldDB; Q06988; -.
DR SMR; Q06988; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; Direct protein sequencing; Lipoprotein;
KW Membrane; Palmitate; Receptor; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8319886"
FT CHAIN 21..599
FT /note="Transferrin-binding protein B"
FT /id="PRO_0000018195"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..119
FT /note="Basic and acidic 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 STRAND 66..71
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4QQ1"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4QQ1"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4QQ1"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 178..195
FT /evidence="ECO:0007829|PDB:4QQ1"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4QQ1"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4QQ1"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4QQ1"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:4QQ1"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 279..297
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 312..323
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 426..438
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:4QQ1"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 463..475
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 553..565
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 567..574
FT /evidence="ECO:0007829|PDB:4QQ1"
FT STRAND 585..594
FT /evidence="ECO:0007829|PDB:4QQ1"
SQ SEQUENCE 599 AA; 65469 MW; B3AE2FBB009AB487 CRC64;
MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVETVQDMH SKPKYEDEKS QPESQQDVSE
NSGAAYGFAV KLPRRNAHFN PKYKEKHKPL GSMDWKKLQR GEPNSFSERD ELEKKRGSSE
LIESKWEDGQ SRVVGYTNFT YVRSGYVYLN KNNIDIKNNI VLFGPDGYLY YKGKEPSKEL
PSEKITYKGT WDYVTDAMEK QRFEGLGSAA GGDKSGALSA LEEGVLRNQA EASSGHTDFG
MTSEFEVDFS DKTIKGTLYR NNRITQNNSE NKQIKTTRYT IQATLHGNRF KGKALAADKG
ATNGSHPFIS DSDSLEGGFY GPKGEELAGK FLSNDNKVAA VFGAKQKDKK DGENAAGPAT
ETVIDAYRIT GEEFKKEQID SFGDVKKLLV DGVELSLLPS EGNKAAFQHE IEQNGVKATV
CCSNLDYMSF GKLSKENKDD MFLQGVRTPV SDVAARTEAN AKYRGTWYGY IANGTSWSGE
ASNQEGGNRA EFDVDFSTKK ISGTLTAKDR TSPAFTITAM IKDNGFSGVA KTGENGFALD
PQNTGNSHYT HIEATVSGGF YGKNAIEMGG SFSFPGNAPE GKQEKASVVF GAKRQQLVQ
