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SIAP_HAEIN
ID   SIAP_HAEIN              Reviewed;         329 AA.
AC   P44542;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Sialic acid-binding periplasmic protein SiaP;
DE   AltName: Full=Extracytoplasmic solute receptor protein SiaP;
DE   AltName: Full=N-acetylneuraminic-binding protein;
DE   AltName: Full=Neu5Ac-binding protein;
DE   Flags: Precursor;
GN   Name=siaP; OrderedLocusNames=HI_0146;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
RN   [3]
RP   FUNCTION, CHARACTERIZATION, SUBUNIT, AND MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=16262798; DOI=10.1111/j.1365-2958.2005.04901.x;
RA   Severi E., Randle G., Kivlin P., Whitfield K., Young R., Moxon R.,
RA   Kelly D., Hood D., Thomas G.H.;
RT   "Sialic acid transport in Haemophilus influenzae is essential for
RT   lipopolysaccharide sialylation and serum resistance and is dependent on a
RT   novel tripartite ATP-independent periplasmic transporter.";
RL   Mol. Microbiol. 58:1173-1185(2005).
RN   [4] {ECO:0007744|PDB:2CEX, ECO:0007744|PDB:2CEY}
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-329 IN COMPLEX WITH SIALIC ACID
RP   ANALOG.
RX   PubMed=16702222; DOI=10.1074/jbc.m603463200;
RA   Mueller A., Severi E., Mulligan C., Watts A.G., Kelly D.J., Wilson K.S.,
RA   Wilkinson A.J., Thomas G.H.;
RT   "Conservation of structure and mechanism in primary and secondary
RT   transporters exemplified by SiaP, a sialic acid binding virulence factor
RT   from Haemophilus influenzae.";
RL   J. Biol. Chem. 281:22212-22222(2006).
RN   [5] {ECO:0007744|PDB:3B50}
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 24-329 IN COMPLEX WITH
RP   N-ACETYL-BETA-NEURAMINATE, FUNCTION, AND MUTAGENESIS OF ASP-72; THR-87;
RP   ARG-150 AND ARG-170.
RC   STRAIN=NTHi 2019;
RX   PubMed=17947229; DOI=10.1074/jbc.m706603200;
RA   Johnston J.W., Coussens N.P., Allen S., Houtman J.C., Turner K.H.,
RA   Zaleski A., Ramaswamy S., Gibson B.W., Apicella M.A.;
RT   "Characterization of the N-acetyl-5-neuraminic acid-binding site of the
RT   extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus
RT   influenzae strain 2019.";
RL   J. Biol. Chem. 283:855-865(2008).
RN   [6] {ECO:0007744|PDB:2XWI, ECO:0007744|PDB:2XWK, ECO:0007744|PDB:2XWO, ECO:0007744|PDB:2XWV}
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 24-329 OF WILD-TYPE AND MUTANTS
RP   ALA-170; GLU-170 AND LYS-170 IN COMPLEX WITH N-ACETYL-BETA-NEURAMINATE,
RP   FUNCTION, AND MUTAGENESIS OF ARG-170.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=26342690; DOI=10.1074/jbc.m115.656603;
RA   Fischer M., Hopkins A.P., Severi E., Hawkhead J., Bawdon D., Watts A.G.,
RA   Hubbard R.E., Thomas G.H.;
RT   "Tripartite ATP-independent Periplasmic (TRAP) Transporters Use an
RT   Arginine-mediated Selectivity Filter for High Affinity Substrate Binding.";
RL   J. Biol. Chem. 290:27113-27123(2015).
CC   -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC       transport system SiaPT involved in the uptake of sialic acid (N-acetyl-
CC       beta-neuraminate). This protein specifically binds sialic acid with
CC       high affinity. N-Acetylneuraminate (sialic acid) can then be
CC       incorporated into the lipooligosaccharides (LOS) as a terminal non-
CC       reducing sugar, protecting the bacterium from complement-mediated
CC       killing by normal human serum. {ECO:0000269|PubMed:16262798,
CC       ECO:0000269|PubMed:17947229, ECO:0000269|PubMed:26342690}.
CC   -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC       protein SiaP, and the fused transmembrane protein SiaT.
CC       {ECO:0000269|PubMed:16262798, ECO:0000269|PubMed:16702222}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=34165; Mass_error=2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16262798};
CC   -!- MISCELLANEOUS: Is essential for lipopolysaccharide (LPS) sialylation
CC       and serum resistance.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC21818.1; -; Genomic_DNA.
DR   PIR; H64143; H64143.
DR   RefSeq; NP_438315.1; NC_000907.1.
DR   PDB; 2CEX; X-ray; 2.20 A; A/B/C/D=24-329.
DR   PDB; 2CEY; X-ray; 1.70 A; A=24-329.
DR   PDB; 2V4C; X-ray; 1.70 A; A=24-329.
DR   PDB; 2WX9; X-ray; 1.37 A; A=24-329.
DR   PDB; 2WYK; X-ray; 1.50 A; A=24-329.
DR   PDB; 2WYP; X-ray; 1.50 A; A=24-329.
DR   PDB; 2XA5; X-ray; 1.09 A; A=24-329.
DR   PDB; 2XWI; X-ray; 2.20 A; A=24-329.
DR   PDB; 2XWK; X-ray; 1.49 A; A=24-329.
DR   PDB; 2XWO; X-ray; 1.54 A; A=24-329.
DR   PDB; 2XWV; X-ray; 1.05 A; A=24-329.
DR   PDB; 2XXK; X-ray; 1.48 A; A=24-329.
DR   PDB; 3B50; X-ray; 1.40 A; A=24-329.
DR   PDB; 6H75; X-ray; 1.45 A; A=24-329.
DR   PDB; 6H76; X-ray; 1.50 A; A=24-329.
DR   PDBsum; 2CEX; -.
DR   PDBsum; 2CEY; -.
DR   PDBsum; 2V4C; -.
DR   PDBsum; 2WX9; -.
DR   PDBsum; 2WYK; -.
DR   PDBsum; 2WYP; -.
DR   PDBsum; 2XA5; -.
DR   PDBsum; 2XWI; -.
DR   PDBsum; 2XWK; -.
DR   PDBsum; 2XWO; -.
DR   PDBsum; 2XWV; -.
DR   PDBsum; 2XXK; -.
DR   PDBsum; 3B50; -.
DR   PDBsum; 6H75; -.
DR   PDBsum; 6H76; -.
DR   AlphaFoldDB; P44542; -.
DR   SMR; P44542; -.
DR   STRING; 71421.HI_0146; -.
DR   TCDB; 2.A.56.1.3; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR   EnsemblBacteria; AAC21818; AAC21818; HI_0146.
DR   KEGG; hin:HI_0146; -.
DR   PATRIC; fig|71421.8.peg.148; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_1_1_6; -.
DR   OMA; FTYKYAN; -.
DR   PhylomeDB; P44542; -.
DR   BioCyc; HINF71421:G1GJ1-158-MON; -.
DR   EvolutionaryTrace; P44542; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 3.40.190.170; -; 1.
DR   InterPro; IPR018389; DctP_fam.
DR   InterPro; IPR004682; TRAP_DctP.
DR   InterPro; IPR038404; TRAP_DctP_sf.
DR   PANTHER; PTHR33376; PTHR33376; 1.
DR   Pfam; PF03480; DctP; 1.
DR   PIRSF; PIRSF006470; DctB; 1.
DR   TIGRFAMs; TIGR00787; dctP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Periplasm; Reference proteome; Signal; Sugar transport;
KW   Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000305"
FT   CHAIN           24..329
FT                   /note="Sialic acid-binding periplasmic protein SiaP"
FT                   /id="PRO_0000031816"
FT   BINDING         33
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   BINDING         72
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   BINDING         90
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   BINDING         150
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   BINDING         170
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   BINDING         210
FT                   /ligand="N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:58705"
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690, ECO:0007744|PDB:2XWV,
FT                   ECO:0007744|PDB:3B50"
FT   MUTAGEN         72
FT                   /note="D->A: Complete loss of incorporation of N-acetyl-
FT                   beta-neuraminate into the LOS."
FT                   /evidence="ECO:0000269|PubMed:17947229"
FT   MUTAGEN         87
FT                   /note="T->R: Complete loss of incorporation of N-acetyl-
FT                   beta-neuraminate into the LOS."
FT                   /evidence="ECO:0000269|PubMed:17947229"
FT   MUTAGEN         150
FT                   /note="R->A: Complete loss of incorporation of N-acetyl-
FT                   beta-neuraminate into the LOS."
FT                   /evidence="ECO:0000269|PubMed:17947229"
FT   MUTAGEN         150
FT                   /note="R->K: Reduced incorporation of N-acetyl-beta-
FT                   neuraminate into the LOS."
FT                   /evidence="ECO:0000269|PubMed:17947229"
FT   MUTAGEN         170
FT                   /note="R->A,K: Complete loss of incorporation of N-acetyl-
FT                   beta-neuraminate into the LOS. Large defect in N-acetyl-
FT                   beta-neuraminate uptake and binding."
FT                   /evidence="ECO:0000269|PubMed:17947229,
FT                   ECO:0000269|PubMed:26342690"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           39..54
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   TURN            66..69
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           91..96
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           99..105
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           124..137
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          139..156
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           161..164
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           175..184
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           212..217
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          234..242
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           251..285
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           296..301
FT                   /evidence="ECO:0007829|PDB:2XWV"
FT   HELIX           303..325
FT                   /evidence="ECO:0007829|PDB:2XWV"
SQ   SEQUENCE   329 AA;  36513 MW;  4E369E0D51DA5F93 CRC64;
     MMKLTKLFLA TAISLGVSSA VLAADYDLKF GMNAGTSSNE YKAAEMFAKE VKEKSQGKIE
     ISLYPSSQLG DDRAMLKQLK DGSLDFTFAE SARFQLFYPE AAVFALPYVI SNYNVAQKAL
     FDTEFGKDLI KKMDKDLGVT LLSQAYNGTR QTTSNRAINS IADMKGLKLR VPNAATNLAY
     AKYVGASPTP MAFSEVYLAL QTNAVDGQEN PLAAVQAQKF YEVQKFLAMT NHILNDQLYL
     VSNETYKELP EDLQKVVKDA AENAAKYHTK LFVDGEKDLV TFFEKQGVKI THPDLVPFKE
     SMKPYYAEFV KQTGQKGESA LKQIEAINP
 
 
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