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TBPB_HAEI8
ID   TBPB_HAEI8              Reviewed;         630 AA.
AC   Q4QLR5;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Transferrin-binding protein B {ECO:0000303|PubMed:28620585};
DE            Short=TbpB {ECO:0000303|PubMed:28620585};
DE   AltName: Full=Transferrin-binding protein 2 {ECO:0000303|PubMed:15968074};
DE   Flags: Precursor;
GN   Name=tbpB {ECO:0000303|PubMed:28620585};
GN   Synonyms=tbp2 {ECO:0000303|PubMed:15968074}; OrderedLocusNames=NTHI1169;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
RN   [2]
RP   TRANSFERRIN-BINDING, AND SUBCELLULAR LOCATION.
RC   STRAIN=86-028NP;
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: Haemophilus 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|PubMed:28620585}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|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}.
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DR   EMBL; CP000057; AAX88032.1; -; Genomic_DNA.
DR   RefSeq; WP_011272339.1; NC_007146.2.
DR   AlphaFoldDB; Q4QLR5; -.
DR   SMR; Q4QLR5; -.
DR   EnsemblBacteria; AAX88032; AAX88032; NTHI1169.
DR   KEGG; hit:NTHI1169; -.
DR   HOGENOM; CLU_024250_0_0_6; -.
DR   OMA; GWFAYPG; -.
DR   OrthoDB; 211030at2; -.
DR   Proteomes; UP000002525; Chromosome.
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   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   Pfam; PF17484; TbpB_A; 1.
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..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..630
FT                   /note="Transferrin-binding protein B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000450811"
FT   REGION          26..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   630 AA;  69327 MW;  9FE74DC161797AF6 CRC64;
     MKSVPLITGG LSFLLSACSG GGGSFDVDDV SNPSSSKPRY QDDTSSSRTK SNLEKLSIPS
     LGGGMKLVAQ NLSGNKEPSF LNENGYISYF SSPSTIEDDV KNVKTENKIH TNPIGLEPNR
     ALQDPNLQKY VYSGLYYIEN WKDFSKLATE KKAYSGHYGY AFYYGNKTAT DLPVSGVATY
     KGTWDFITAT KYGQNYSLFS NARGQAYFRR SATRGDIDLE NNSKNGDIGL ISEFSADFGT
     KKLTGQLSYT KRKTDIQQYE KEKLYDIDAH IYSNRFRGKV TPTKSTSDEH PFTSEGTLEG
     GFYGPNAEEL GGKFLARDKR VFGVFSAKET PETEKEKLSK ETLIDGKLIT FSTKTADATT
     STTASTTADV KTDEKNFTTK DISSFGEADY LLIDNYPVPL FPEGDTDDFV TSKHHDIGNK
     TYKVEACCKN LSYVKFGMYY EDKEKKNTNQ TGQYHQFLLG LRTPSSQIPV TGNVKYLGSW
     FGYIGDDKTS YSTTGNKQQD KNAPAEFDVN FDNKTLTGKL KRADSQNTVF NIEATFKNGS
     NAFEGKATAN VVIDPKNTQA TSKVNFTTTV NGAFYGPHAT ELGGYFTYNG NNPTATNSES
     SSTVPSPPNS PNARAAVVFG AKRQVEKTNK
 
 
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