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