ID   TBPB_MORCA              Reviewed;         706 AA.
AC   P0DTW7;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Transferrin-binding protein B {ECO:0000303|PubMed:28620585};
DE            Short=TbpB {ECO:0000303|PubMed:28620585};
DE   Flags: Precursor;
GN   Name=tbpB {ECO:0000303|PubMed:21269504}; ORFNames=EA1_03415;
OS   Moraxella catarrhalis (Branhamella catarrhalis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O53E;
RX   PubMed=21269504; DOI=10.1186/1471-2164-12-70;
RA   Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J.,
RA   Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P.,
RA   Campagnari A.A.;
RT   "Comparative analysis and supragenome modeling of twelve Moraxella
RT   catarrhalis clinical isolates.";
RL   BMC Genomics 12:70-70(2011).
RN   [2]
RP   TRANSFERRIN-BINDING, AND SUBCELLULAR LOCATION.
RC   STRAIN=O53E;
RX   PubMed=28620585; DOI=10.3389/fcimb.2017.00207;
RA   Hooda Y., Lai C.C.L., Moraes T.F.;
RT   "Identification of a Large Family of Slam-Dependent Surface Lipoproteins in
RT   Gram-Negative Bacteria.";
RL   Front. Cell. Infect. Microbiol. 7:207-207(2017).
CC   -!- FUNCTION: Moraxella acquires iron by extracting it from serum
CC       transferrin (TF) in its human host. Acts as a transferrin receptor and
CC       is required for transferrin utilization. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000305|PubMed:28620585}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}. Cell surface
CC       {ECO:0000269|PubMed:28620585}. Note=When expressed in E.coli.
CC       {ECO:0000269|PubMed:28620585}.
CC   -!- SIMILARITY: Belongs to the TbpB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AERL01000018; EGE27321.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DTW7; -.
DR   SMR; P0DTW7; -.
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; 2.
DR   Pfam; PF01298; TbpB_B_D; 2.
DR   Pfam; PF17483; TbpB_C; 1.
DR   SUPFAM; SSF56925; SSF56925; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..706
FT                   /note="Transferrin-binding protein B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000450812"
FT   REGION          26..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   706 AA;  76351 MW;  DDDDA4457A8342C3 CRC64;
     MKHIPLTTLC VAISAVLLTA CGGSGGSNPP APTPIPNASG SGNTGNTGNA GGTDNTANAG
     NTGGASSGTG SANTPEPKYQ DVPTDKNEKE QVSPIQEPAM GYGMALSKIN LHNRQDTPLD
     EKNIITLDGK KQVAEGKKSP LPFSLDVENK LLDGYIAKMD KADKNAIRRR IESENKAKPL
     SEAELAEKIK EAVRKSYEFQ QVMTSLENKI FHSNDGTTKA TTRDLQYVDY GYYLANDANY
     LTVKTDKPKL WNSGPVGGVF YNGSTTAKEL PTQDAVKYKG HWDFMTDVAN KGNRFSEVKG
     TRQAGWWYGA SSKDEYNRLL TDEKNKPDGY NGEYGHSSEF TVNFKEKKLT GGLFSNLQDS
     HKQKVTKTKR YDIDANIHGN RFRGSAIASD KEKDSETKHP FTSDAKDRLE GGFYGPKGEE
     LAGKFLTDDN KLFGVFGAKQ ESKADKTEAI LDAYALGAFN KNDANTFTPF TKKQLDNFGN
     AKKLVLGSTV INLVSTDATK NEFTEDKPKS ATNKAGETLM VNDKVSVKTY GYGRNFEYLK
     FGELSVGGSH SVFLQGERTA TTGDKAVPTE GKAKYLGNWV GYITGTGTGK SFNEAQDIAD
     FDIDFKNKTV NGKLTTKGRT DPVFNITGEI SGNGWTGKAS TAKADAGGYN IDSNGTNKSI
     VIRDADVTGG FYGPNATEMG GSFTHNTNDS KASVVFGTKR QEEVKP