PHBP_UNKP
ID PHBP_UNKP Reviewed; 376 AA.
AC P85173;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Phosphate-binding protein;
DE Short=HPBP;
OS Unknown prokaryotic organism.
OC Bacteria; environmental samples.
OX NCBI_TaxID=2725;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=18076037; DOI=10.1002/prot.21866;
RA Diemer H., Elias M., Renault F., Rochu D., Contreras-Martel C.,
RA Schaeffer C., Van Dorsselaer A., Chabriere E.;
RT "Tandem use of X-ray crystallography and mass spectrometry to obtain ab
RT initio the complete and exact amino acids sequence of HPBP, a human 38-kDa
RT apolipoprotein.";
RL Proteins 71:1708-1720(2008).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-33; 38-125; 127-152; 197-230; 246-298; 313-321;
RP 332-347 AND 356-372, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), INTERACTION
RP WITH HUMAN PON1, DISULFIDE BONDS, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Plasma {ECO:0000269|PubMed:16531243};
RX PubMed=16531243; DOI=10.1016/j.str.2005.12.012;
RA Morales R., Berna A., Carpentier P., Contreras-Martel C., Renault F.,
RA Nicodeme M., Chesne-Seck M.-L., Bernier F., Dupuy J., Schaeffer C.,
RA Diemer H., van Dorsselaer A., Fontecilla-Camps J.C., Masson P., Rochu D.,
RA Chabriere E.;
RT "Serendipitous discovery and X-ray structure of a human phosphate binding
RT apolipoprotein.";
RL Structure 14:601-609(2006).
CC -!- FUNCTION: Phosphate-binding protein. {ECO:0000269|PubMed:18076037}.
CC -!- SUBUNIT: Heterooligomer with human PON1.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16531243}.
CC -!- TISSUE SPECIFICITY: Found in human plasma.
CC {ECO:0000269|PubMed:16531243}.
CC -!- MASS SPECTROMETRY: Mass=38529.11; Mass_error=0.06; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18076037};
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
CC -!- CAUTION: Although this is said to be a human protein, it is not encoded
CC in the human genome. It is highly similar to microbial proteins and
CC belongs to a family of microbial proteins. {ECO:0000305}.
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DR PDB; 2V3Q; X-ray; 1.89 A; A=1-376.
DR PDB; 3W9V; X-ray; 1.03 A; A/B=1-376.
DR PDB; 3W9W; X-ray; 1.35 A; A/B=1-376.
DR PDB; 4M1V; X-ray; 1.30 A; A=1-376.
DR PDBsum; 2V3Q; -.
DR PDBsum; 3W9V; -.
DR PDBsum; 3W9W; -.
DR PDBsum; 4M1V; -.
DR AlphaFoldDB; P85173; -.
DR SMR; P85173; -.
DR PRIDE; P85173; -.
DR EvolutionaryTrace; P85173; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR024370; PBP_domain.
DR Pfam; PF12849; PBP_like_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Phosphate transport; Secreted; Transport.
FT CHAIN 1..376
FT /note="Phosphate-binding protein"
FT /id="PRO_0000295168"
FT DISULFID 113..158
FT /evidence="ECO:0000269|PubMed:16531243"
FT DISULFID 306..369
FT /evidence="ECO:0000269|PubMed:16531243"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3W9V"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3W9V"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3W9V"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:3W9V"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3W9V"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:3W9V"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:3W9V"
SQ SEQUENCE 376 AA; 38533 MW; 7D492A5FE3E18A49 CRC64;
DINGGGATLP QKLYLTPDVL TAGFAPYIGV GSGKGKIAFL ENKYNQFGTD TTKNVHWAGS
DSKLTATELA TYAADKEPGW GKLIQVPSVA TSVAIPFRKA GANAVDLSVK ELCGVFSGRI
ADWSGITGAG RSGPIQVVYR AESSGTTELF TRFLNAKCTT EPGTFAVTTT FANSYSLGLT
PLAGAVAATG SDGVMAALND TTVAEGRITY ISPDFAAPTL AGLDDATKVA RVGKGVVNGV
AVEGKSPAAA NVSAAISVVP LPAAADRGNP DVWVPVFGAT TGGGVVAYPD SGYPILGFTN
LIFSQCYANA TQTGQVRDFF TKHYGTSANN DAAIEANAFV PLPSNWKAAV RASFLTASNA
LSIGNTNVCN GKGRPQ
