ID   TBPA2_NEIMI             Reviewed;         908 AA.
AC   Q06987;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transferrin-binding protein A {ECO:0000305};
DE            Short=TbpA {ECO:0000305};
DE   AltName: Full=Transferrin-binding protein 1 {ECO:0000303|PubMed:8344530};
DE   Flags: Precursor;
GN   Name=tbp1 {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 25-42, AND
RP   SUBCELLULAR 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 25-45.
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).
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:0000250|UniProtKB:Q9K0U9}.
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:0000250|UniProtKB:Q9K0U9}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:8344530};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9K0U9}.
CC   -!- INDUCTION: By iron starvation.
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; Z15129; CAA78831.1; -; Genomic_DNA.
DR   PIR; JN0819; JN0819.
DR   AlphaFoldDB; Q06987; -.
DR   SMR; Q06987; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0071702; P:organic substance transport; IEA:UniProt.
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   Cell outer membrane; Direct protein sequencing; Membrane; Receptor; Signal;
KW   TonB box; Transmembrane; Transmembrane beta strand; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:8319886,
FT                   ECO:0000269|PubMed:8344530"
FT   CHAIN           25..908
FT                   /note="Transferrin-binding protein A"
FT                   /id="PRO_0000034775"
FT   MOTIF           38..45
FT                   /note="TonB box"
FT   MOTIF           891..908
FT                   /note="TonB C-terminal box"
SQ   SEQUENCE   908 AA;  101583 MW;  FE2FF4974CAC3C31 CRC64;
     MQQQHLFRLN ILCLSLMTAL PVYAENVQAE QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK
     LVKSSDTLSK EQVLNIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVS LTVDGVSQIQ
     SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSS EYGNGALAGS VAFQTKTAAD
     IIGEGKQWGI QSKTAYSGKD HALTQSLALA GRSGGAEALL IYTKRRGREI HAHKDAGKGV
     QSFNRLVLDE DKKEGGSQYR YFIVEEECHN GYAACKNKLK EDASVKDERK TVSTQDYTGS
     NRLLANPLEY GSQSWLFRPG WHLDNRHYVG AVLERTQQTF DTRDMTVPAY FTSEDYVPGS
     LKGLGKYSGD NKAERLFVQG EGSTLQGIGY GTGVFYDERH TKNRYGVEYV YHNADKDTWA
     DYARLSYDRQ GIDLDNRLQQ THCSHDGSDK NCRPDGNKPY SFYKSDRMIY EESRNLFQAV
     FKKAFDTAKI RHNLSINLGY DRFKSQLSHS DYYLQNAVQA YDLITPKKPP FPNGSKDNPY
     RVSIGKTTVN TSPICRFGNN TYTDCTPRNI GGNGYYAAVQ DNVRLGRWAD VGAGIRYDYR
     STHSEDKSVS TGTHRNLSWN AGVVLKPFTW MDLTYRASTG FRLPSFAEMY GWRAGESLKT
     LDLKPEKSFN REAGIVFKGD FGNLEASYFN NAYRDLIAFG YETRTQNGQT SASGDPGYRN
     AQNARIAGIN ILGKIDWHGV WGGLPDGLYS TLAYNRIKVK DADIRADRTF VTSYLFDAVQ
     PSRYVLGLGY DHPDGIWGIN TMFTYSKAKS VDELLGSQAL LNGNANAKKA ASRRTRPWYV
     TDVSGYYNIK KHLTLRAGVY NLLNYRYVTW ENVRQTAGGA VNQHKNVGVY NRYAAPGRNY
     TFSLEMKF