SIAM_VIBCH
ID SIAM_VIBCH Reviewed; 427 AA.
AC Q9KR66;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Sialic acid TRAP transporter large permease protein SiaM {ECO:0000305};
GN Name=siaM {ECO:0000303|PubMed:22167185};
GN OrderedLocusNames=VC_1777 {ECO:0000312|EMBL:AAF94926.1};
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, SUBUNIT, AND SUBCELLULAR LOCATION.
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, AND DISRUPTION PHENOTYPE.
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. {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. SiaQ
CC and SiaM form a tight 1:1 complex. {ECO:0000269|PubMed:22167185}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22167185}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to grow on N-
CC acetylneuraminic acid (Neu5Ac) as the sole carbon source.
CC {ECO:0000269|PubMed:22556361}.
CC -!- SIMILARITY: Belongs to the TRAP transporter large permease family.
CC {ECO:0000305}.
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DR EMBL; AE003852; AAF94926.1; -; Genomic_DNA.
DR PIR; F82157; F82157.
DR RefSeq; NP_231412.1; NC_002505.1.
DR RefSeq; WP_000233105.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KR66; -.
DR SMR; Q9KR66; -.
DR STRING; 243277.VC_1777; -.
DR DNASU; 2613657; -.
DR EnsemblBacteria; AAF94926; AAF94926; VC_1777.
DR GeneID; 57740421; -.
DR KEGG; vch:VC_1777; -.
DR PATRIC; fig|243277.26.peg.1697; -.
DR eggNOG; COG1593; Bacteria.
DR HOGENOM; CLU_019824_4_1_6; -.
DR OMA; GMGHVNI; -.
DR BioCyc; VCHO:VC1777-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR010656; DctM.
DR InterPro; IPR004681; TRAP_DctM.
DR PANTHER; PTHR33362; PTHR33362; 1.
DR Pfam; PF06808; DctM; 1.
DR PIRSF; PIRSF006066; HI0050; 1.
DR TIGRFAMs; TIGR00786; dctM; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..427
FT /note="Sialic acid TRAP transporter large permease protein
FT SiaM"
FT /id="PRO_0000435368"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 45457 MW; 77124470ADA8346D CRC64;
MVGSIFGWLG LLFAGMPVGF SLIFVALAFL ILTNSTGINF AAQQMLGGID NFTLLAVPFF
VLTGHLMNSA GITERIFNFA KSLVGHITGS LGHVNIMASL LFSGMSGSAL ADAGGLGQLE
IKSMRDAKYH DDFAGGLTAA SCIIGPLVPP SVPLVIYGVV SNTSIGALFL AGAIPGLLCC
IALMVMSYFI CKKRGYMTLP KASRREQFKS LKEAFLSLLT PVIIIGGIFS GKFTPTEAAA
VSSLYALFLG TVVYNTLTLQ GFIEILKETV NTTAVVALMV MGVTVFGWIV AREQLPQMLA
DYFLTISDNP LVLLLLINLL LLFLGTFIES LALLLLLVPF LVPVASAVGI DPVHFGVMAI
LNLMIGILTP PMGMALYVVS RVGDIPFHTL TRGVLPLLVP LFIVLALVAV FPQFTLLLPE
LFLGYGQ
