SIAP_VIBCH
ID SIAP_VIBCH Reviewed; 321 AA.
AC Q9KR64;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Sialic acid-binding periplasmic protein SiaP {ECO:0000305};
DE Flags: Precursor;
GN Name=siaP {ECO:0000303|PubMed:22167185};
GN OrderedLocusNames=VC_1779 {ECO:0000312|EMBL:AAF94928.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22167185; DOI=10.1074/jbc.m111.281030;
RA Mulligan C., Leech A.P., Kelly D.J., Thomas G.H.;
RT "The membrane proteins SiaQ and SiaM form an essential stoichiometric
RT complex in the sialic acid tripartite ATP-independent periplasmic (TRAP)
RT transporter SiaPQM (VC1777-1779) from Vibrio cholerae.";
RL J. Biol. Chem. 287:3598-3608(2012).
RN [3]
RP FUNCTION.
RX PubMed=22556361; DOI=10.1099/mic.0.059659-0;
RA Chowdhury N., Norris J., McAlister E., Lau S.Y., Thomas G.H., Boyd E.F.;
RT "The VC1777-VC1779 proteins are members of a sialic acid-specific subfamily
RT of TRAP transporters (SiaPQM) and constitute the sole route of sialic acid
RT uptake in the human pathogen Vibrio cholerae.";
RL Microbiology 158:2158-2167(2012).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system SiaPQM that catalyzes unidirectional Na(+)-dependent
CC sialic acid uptake. Binds the common sialic acid N-acetylneuraminic
CC acid (Neu5Ac) with a high affinity. {ECO:0000269|PubMed:22167185,
CC ECO:0000269|PubMed:22556361}.
CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC protein SiaP, and the two transmembrane proteins SiaQ and SiaM.
CC {ECO:0000269|PubMed:22167185}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000305}.
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DR EMBL; AE003852; AAF94928.1; -; Genomic_DNA.
DR PIR; H82157; H82157.
DR RefSeq; NP_231414.1; NC_002505.1.
DR RefSeq; WP_000849284.1; NZ_LT906614.1.
DR PDB; 5LTC; X-ray; 2.10 A; A/B=22-321.
DR PDB; 7A5C; X-ray; 2.20 A; A/B=23-321.
DR PDB; 7A5Q; X-ray; 1.68 A; A/B=23-321.
DR PDBsum; 5LTC; -.
DR PDBsum; 7A5C; -.
DR PDBsum; 7A5Q; -.
DR AlphaFoldDB; Q9KR64; -.
DR SMR; Q9KR64; -.
DR STRING; 243277.VC_1779; -.
DR TCDB; 2.A.56.1.6; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR PRIDE; Q9KR64; -.
DR DNASU; 2613659; -.
DR EnsemblBacteria; AAF94928; AAF94928; VC_1779.
DR GeneID; 57740423; -.
DR KEGG; vch:VC_1779; -.
DR PATRIC; fig|243277.26.peg.1699; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_1_6; -.
DR OMA; FTYKYAN; -.
DR BioCyc; VCHO:VC1779-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..321
FT /note="Sialic acid-binding periplasmic protein SiaP"
FT /id="PRO_5004328968"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:7A5Q"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:7A5Q"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:7A5Q"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 136..153
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 248..282
FT /evidence="ECO:0007829|PDB:7A5Q"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 293..310
FT /evidence="ECO:0007829|PDB:7A5Q"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:7A5Q"
SQ SEQUENCE 321 AA; 35982 MW; C1A44BB820F595F0 CRC64;
MKTINKITIA ILTLSAAASV NAATTLKMGM QASVGSVEYN SAKMLADTLE EMSQGEIKLA
LYPSAQLGDD RAMLQQLTLG DLDITYAEFG RMGLWIPRAE AVMLPYVAKD FDHLRRMFES
DFGQGVRDEM LQKFNWRALD TWYNGTRETT SNRPLNSIED FKGLKLRVPN AKQNLNYAKL
SGASPTPMSF SEVYLALQTN AVDGQENPLP TIKTMKFYEV QKNLAMTHHI VNDQMVIISE
STWQKLSDTD KDIIQKAVQK VGDAHTQTVK TQEAELVSFF KSEGINVTYP DLEPFREAMQ
PLYKEFDSNI GQPIVSKLAA M
