ID   TBPB_NEIMA              Reviewed;         698 AA.
AC   O68937; A1ITL3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Transferrin-binding protein B {ECO:0000303|PubMed:10067678};
DE            Short=TbpB {ECO:0000303|PubMed:10067678};
DE   AltName: Full=Transferrin-binding protein 2;
DE            Short=TBP-2;
DE   Flags: Precursor;
GN   Name=tbpB {ECO:0000303|PubMed:10067678}; Synonyms=tbp2;
GN   OrderedLocusNames=NMA2025;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10067678; DOI=10.1016/s0264-410x(98)00257-6;
RA   Brieske N., Schenker M., Schnibbe T., Quentin-Millet M.-J., Achtman M.;
RT   "Human antibody responses to A and C capsular polysaccharides, IgA1
RT   protease and transferrin-binding protein complex stimulated by infection
RT   with Neisseria meningitidis of subgroup IV-1 or ET-37 complex.";
RL   Vaccine 17:731-744(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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).
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}.
CC   -!- SUBUNIT: Binds only human holo-transferrin (TF), via the TF C-terminus.
CC       Forms a large complex with TbpA and TF (By similarity). Interacts via
CC       its C-terminal domain with Slam1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q06988, ECO:0000250|UniProtKB:Q9K0V0}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Cell surface {ECO:0000250|UniProtKB:Q06988}.
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. {ECO:0000305}.
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DR   EMBL; AF058689; AAC13725.1; -; Genomic_DNA.
DR   EMBL; AL157959; CAM09130.1; -; Genomic_DNA.
DR   PIR; D81832; D81832.
DR   RefSeq; WP_002246892.1; NC_003116.1.
DR   AlphaFoldDB; O68937; -.
DR   SMR; O68937; -.
DR   PRIDE; O68937; -.
DR   EnsemblBacteria; CAM09130; CAM09130; NMA2025.
DR   KEGG; nma:NMA2025; -.
DR   HOGENOM; CLU_024250_0_0_4; -.
DR   OMA; GWFAYPG; -.
DR   BioCyc; NMEN122587:NMA_RS10275-MON; -.
DR   Proteomes; UP000000626; Chromosome.
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   3: Inferred from homology;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Receptor; Signal;
KW   Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..698
FT                   /note="Transferrin-binding protein B"
FT                   /id="PRO_0000018192"
FT   REGION          33..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..688
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"
SQ   SEQUENCE   698 AA;  75176 MW;  83FBE14DDF617B1F CRC64;
     MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVSSE KPQAQKDQGG
     YGFAMRLKRR NWYRQANPKE DEIKLSENDW EQTDNGDIKN PSKQKNIINA LTGNNGGASL
     QDSSQENQGI SKVTGHHNFQ YVWSGFFYKQ IGSTFERKDS SITAARSGPD GYIFYKGKDP
     SRKLPVSGEV MYKGTWDFLT DVKTSQKFTD LGNTSTRPGD RYSAFSGELD YIVNKDSDKK
     DEHVGWGLTT EITVDFEKKT LSGKLIKNNR VNNDNDKHTT QYYSLDATLR GNRFSGKAEA
     TDKPKNDGET KEHPFVSDSS SLSGGFFGPK GEELGFRFLS DDQKVAVVGS AKTQDKPRNG
     AVASGGAGAA ASNGAAGTSS ENSKLTTVLD AVELTLNDKK IKNLDNFSNA AQLVVDGIMI
     PLLPEASESG KNQANQGTNG GTAFTRKFNH TPKSDEKDTQ AGTAENGNPA ASNTAGDANG
     KTKTYEVEVC CSNLNYLKYG MLTRKNSKSA MQAGESSSQA DAKTEQVGQS MFLQGERTDE
     KEIPNDQNVV YRGSWYGHIA NGTSWSGNAS DKEGGNRADF TVNFGTKKIN GTLTADNRQA
     ATFTIVGDIE GNGFSGTAKT ADSGFDLDQS NNTRTPKAYI TNAKVQGGFY GPKAEELGGW
     FAYSDDKQTK NATDASGNGN SASSATVVFG AKRQKPVQ