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TBPA1_NEIMI
ID   TBPA1_NEIMI             Reviewed;         911 AA.
AC   Q09056;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
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 25-38 AND 133-149,
RP   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).
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; Z15130; CAA78833.1; -; Genomic_DNA.
DR   PIR; JN0821; JN0821.
DR   AlphaFoldDB; Q09056; -.
DR   SMR; Q09056; -.
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:8344530"
FT   CHAIN           25..911
FT                   /note="Transferrin-binding protein A"
FT                   /id="PRO_0000034774"
FT   MOTIF           38..45
FT                   /note="TonB box"
FT   MOTIF           894..911
FT                   /note="TonB C-terminal box"
SQ   SEQUENCE   911 AA;  101631 MW;  99283ABAE0B773E6 CRC64;
     MQQQHLFRLN ILCLSLMTAL PAYAENVQAG QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK
     LVKTADTLSK EQVLDIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVS LTVDGLAQIQ
     SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSV EQGSGALAGS VAFQTKTADD
     VIGEGRQWGI QSKTAYSGKN RGLTQSIALA GRIGGAEALL IHTGRRAGEI RAHEDAGRGV
     QSFNRLVPVE DSSEYAYFIV EDECEGKNYE TCKSKPKKDV VGKDERQTVS TRDYTGPNRF
     LADPLSYESR SWLFRPGFRF ENKRHYIGGI LEHTQQTFDT RDMTVPAFLT KAVFDANSKQ
     AGSLPGNGKY AGNHKYGGLF TNGENGALVG AEYGTGVFYD ETHTKSRYGL EYVYTNADKD
     TWADYARLSY DRQGIGLDNH FQQTHCSADG SDKYCRPSAD KPFSYYKSDR VIYGESHRLL
     QAAFKKSFDT AKIRHNLSVN LGFDRFDSNL RHQDYYYQHA NRAYSSKTPP KTANPNGDKS
     KPYWVSIGGG NVVTGQICLF GNNTYTDCTP RSINGKSYYA AVRDNVRLGR WADVGAGLRY
     DYRSTHSDDG SVSTGTHRTL SWNAGIVLKP ADWLDLTYRT STGFRLPSFA EMYGWRSGVQ
     SKAVKIDPEK SFNKEAGIVF KGDFGNLEAS WFNNAYRDLI VRGYEAQIKN GKEEAKGDPA
     YLNAQSARIT GINILGKIDW NGVWDKLPEG WYSTFAYNRV HVRDIKKRAD RTDIQSHLFD
     AIQPSRYVVG LGYDQPEGKW GVNGMLTYSK AKEITELLGS RALLNGNSRN TKATARRTRP
     WYIVDVSGYY TIKKHFTLRA GVYNLLNYRY VTWENVRQTA GGAVNQHKNV GVYNRYAAPG
     RNYTFSLEMK F
 
 
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