ID   TBPA_NEIGO              Reviewed;         915 AA.
AC   Q01996;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Transferrin-binding protein A {ECO:0000305};
DE            Short=TbpA;
DE   AltName: Full=Transferrin-binding protein 1 {ECO:0000303|PubMed:1325963};
DE   Flags: Precursor;
GN   Name=tbpA {ECO:0000303|PubMed:1325963};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FA19;
RX   PubMed=1325963; DOI=10.1128/jb.174.18.5788-5797.1992;
RA   Cornelissen C.N., Biswas G.D., Tsai J., Paruchuri D.K., Thompson S.A.,
RA   Sparling P.F.;
RT   "Gonococcal transferrin-binding protein 1 is required for transferrin
RT   utilization and is homologous to TonB-dependent outer membrane receptors.";
RL   J. Bacteriol. 174:5788-5797(1992).
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
CC       {ECO:0000250|UniProtKB:Q9K0U9}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9K0U9}.
CC   -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC       {ECO:0000305}.
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DR   EMBL; M96731; AAA25503.1; -; Genomic_DNA.
DR   PIR; A43335; A43335.
DR   RefSeq; WP_003693614.1; NZ_CP012026.1.
DR   AlphaFoldDB; Q01996; -.
DR   SMR; Q01996; -.
DR   PRIDE; Q01996; -.
DR   PATRIC; fig|485.48.peg.1488; -.
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   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Receptor; Signal; TonB box; Transmembrane;
KW   Transmembrane beta strand; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..915
FT                   /note="Transferrin-binding protein A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000034773"
FT   REGION          526..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           38..45
FT                   /note="TonB box"
FT   MOTIF           898..915
FT                   /note="TonB C-terminal box"
FT   COMPBIAS        526..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  102213 MW;  697CF74B1010422F CRC64;
     MQQQHLFRLN ILCLSLMTAL PAYAENVQAG QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK
     LVKTADTLSK EQVLDIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVS LTVDGLAQIQ
     SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSV EQGSGALAGS VAFQTKTADD
     VIGEGRQWGI QSKTAYSGKN RGLTQSIALA GRIGGAEALL IRTGRHAGEI RAHEAAGRGV
     QSFNRLAPVD DGSKYAYFIV EEECKNGGHE KCKANPKKDV VGEDKRQTVS TRDYTGPNRF
     LADPLSYESR SWLFRPGFRF ENKRHYIGGI LERTQQTFDT RDMTVPAFLT KAVFDANQKQ
     AGSLRGNGKY AGNHKYGGLF TSGENNAPVG AEYGTGVFYD ETHTKSRYGL EYVYTNADKD
     TWADYARLSY DRQGIGLDNH FQQTHCSADG SDKYCRPSAD KPFSYYKSDR VIYGESHKLL
     QAAFKKSFDT AKIRHNLSVN LGYDRFGSNL RHQDYYYQSA NRAYSLKTPP QNNGKKTSPN
     GREKNPYWVS IGRGNVVTRQ ICLFGNNTYT DCTPRSINGK SYYAAVRDNV RLGRWADVGA
     GLRYDYRSTH SDDGSVSTGT HRTLSWNAGI VLKPADWLDL TYRTSTGFRL PSFAEMYGWR
     SGDKIKAVKI DPEKSFNKEA GIVFKGDFGN LEASWFNNAY RDLIVRGYEA QIKDGKEQVK
     GNPAYLNAQS ARITGINILG KIDWNGVWDK LPEGWYSTFA YNRVRVRDIK KRADRTDIQS
     HLFDAIQPSR YVVGSGYDQP EGKWGVNGML TYSKAKEITE LLGSRALLNG NSRNTKATAR
     RTRPWYIVDV SGYYTVKKHF TLRAGVYNLL NHRYVTWENV RQTAAGAVNQ HKNVGVYNRY
     AAPGRNYTFS LEMKF