TBPB1_NEIMI
ID TBPB1_NEIMI Reviewed; 711 AA.
AC Q09057;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Transferrin-binding protein B {ECO:0000305};
DE Short=TbpB {ECO:0000305};
DE AltName: Full=TbpB receptor {ECO:0000303|PubMed:22343719};
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 22-33; 58-66;
RP 144-162 AND 178-192, TRANSFERRIN-BINDING, AND SUBCELLULAR LOCATION.
RC STRAIN=CCUG 37608 / M982 / Serogroup B / Serotype 9;
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 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] {ECO:0007744|PDB:3VE1, ECO:0007744|PDB:3VE2}
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 56-711 ALONE AND IN COMPLEX WITH
RP HUMAN TRANSFERRIN, FUNCTION, TRANSFERRIN-BINDING, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF ARG-219 AND GLU-241.
RC STRAIN=CCUG 37608 / M982 / Serogroup B / Serotype 9;
RX PubMed=22343719; DOI=10.1038/nsmb.2251;
RA Calmettes C., Alcantara J., Yu R.H., Schryvers A.B., Moraes T.F.;
RT "The structural basis of transferrin sequestration by transferrin-binding
RT protein B.";
RL Nat. Struct. Mol. Biol. 19:358-360(2012).
RN [4] {ECO:0007744|PDB:5KKX}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 396-711.
RA Fegan J.E., Calmettes C., Yu R.-H., Moraes T.F.M., Schryvers A.B.;
RT "Engineered hybrid transferrin binding protein antigens for protection
RT against Neisseria meningitidis.";
RL Submitted (JUN-2016) to the PDB data bank.
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:22343719}.
CC -!- SUBUNIT: Binds only human holo-transferrin (TF), via the TF C-terminus
CC (PubMed:22343719). Forms a large complex with TbpA and TF (By
CC similarity). Interacts via its C-terminal domain with Slam1 (By
CC similarity). {ECO:0000250|UniProtKB:Q06988,
CC ECO:0000250|UniProtKB:Q9K0V0, ECO:0000269|PubMed:22343719}.
CC -!- INTERACTION:
CC Q09057; P02787: TF; Xeno; NbExp=3; IntAct=EBI-15970048, EBI-714319;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:8344530};
CC Lipid-anchor {ECO:0000305|PubMed:8344530}. Cell surface
CC {ECO:0000269|PubMed:8344530, ECO:0000305|PubMed:22343719}.
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. TbpB stabilizes the TF
CC holo C-terminal lobe's conformation. {ECO:0000269|PubMed:22343719}.
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; Z15130; CAA78832.1; -; Genomic_DNA.
DR PIR; JN0820; JN0820.
DR PDB; 3VE1; X-ray; 2.96 A; A/C=56-711.
DR PDB; 3VE2; X-ray; 2.14 A; A/B=56-711.
DR PDB; 5KKX; X-ray; 2.10 A; A/B=396-711.
DR PDBsum; 3VE1; -.
DR PDBsum; 3VE2; -.
DR PDBsum; 5KKX; -.
DR AlphaFoldDB; Q09057; -.
DR SMR; Q09057; -.
DR DIP; DIP-59922N; -.
DR IntAct; Q09057; 1.
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 CHAIN 21..711
FT /note="Transferrin-binding protein B"
FT /id="PRO_0000018194"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..492
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 219
FT /note="R->A: Wild-type binding to human transferrin."
FT /evidence="ECO:0000269|PubMed:22343719"
FT MUTAGEN 241
FT /note="E->R: Dramatically reduced binding to human
FT transferrin."
FT /evidence="ECO:0000269|PubMed:22343719"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3VE2"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3VE1"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3VE2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3VE2"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3VE1"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3VE1"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3VE2"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:3VE2"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3VE2"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:3VE2"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:3VE2"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3VE1"
FT STRAND 294..305
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3VE2"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:5KKX"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 508..519
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 541..550
FT /evidence="ECO:0007829|PDB:5KKX"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 560..580
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:5KKX"
FT TURN 597..600
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:5KKX"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:3VE1"
FT STRAND 615..623
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 626..632
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:5KKX"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 669..677
FT /evidence="ECO:0007829|PDB:5KKX"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:5KKX"
FT STRAND 697..706
FT /evidence="ECO:0007829|PDB:5KKX"
SQ SEQUENCE 711 AA; 76928 MW; A152654C1F5BFD85 CRC64;
MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVSSE KPQAQKDQGG
YGFAMRLKRR NWYPGAEESE VKLNESDWEA TGLPTKPKEL PKRQKSVIEK VETDGDSDIY
SSPYLTPSNH QNGSAGNGVN QPKNQATGHE NFQYVYSGWF YKHAASEKDF SNKKIKSGDD
GYIFYHGEKP SRQLPASGKV IYKGVWHFVT DTKKGQDFRE IIQPSKKQGD RYSGFSGDGS
EEYSNKNEST LKDDHEGYGF TSNLEVDFGN KKLTGKLIRN NASLNNNTNN DKHTTQYYSL
DAQITGNRFN GTATATDKKE NETKLHPFVS DSSSLSGGFF GPQGEELGFR FLSDDQKVAV
VGSAKTKDKL ENGAAASGST GAAASGGAAG TSSENSKLTT VLDAVELTLN DKKIKNLDNF
SNAAQLVVDG IMIPLLPKDS ESGNTQADKG KNGGTEFTRK FEHTPESDKK DAQAGTQTNG
AQTASNTAGD TNGKTKTYEV EVCCSNLNYL KYGMLTRKNS KSAMQAGGNS SQADAKTEQV
EQSMFLQGER TDEKEIPTDQ NVVYRGSWYG HIANGTSWSG NASDKEGGNR AEFTVNFADK
KITGKLTAEN RQAQTFTIEG MIQGNGFEGT AKTAESGFDL DQKNTTRTPK AYITDAKVKG
GFYGPKAEEL GGWFAYPGDK QTEKATATSS DGNSASSATV VFGAKRQQPV Q
