SCRY_SALTM
ID SCRY_SALTM Reviewed; 505 AA.
AC P22340;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Sucrose porin;
DE Flags: Precursor;
GN Name=scrY;
OS Salmonella typhimurium.
OG Plasmid pUR400.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-33.
RC STRAIN=6153-62;
RX PubMed=1846143; DOI=10.1128/jb.173.2.449-456.1991;
RA Hardesty C., Ferran C., DiRienzo J.M.;
RT "Plasmid-mediated sucrose metabolism in Escherichia coli: characterization
RT of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose
RT phosphotransferase system outer membrane porin.";
RL J. Bacteriol. 173:449-456(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1649946; DOI=10.1111/j.1365-2958.1991.tb00769.x;
RA Schmid K., Ebner R., Jahreis K., Lengeler J.W., Titgemeyer F.;
RT "A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric
RT bacteria.";
RL Mol. Microbiol. 5:941-950(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9437428; DOI=10.1038/nsb0198-37;
RA Forst D., Welte W., Wacker T., Diederichs K.;
RT "Structure of the sucrose-specific porin ScrY from Salmonella typhimurium
RT and its complex with sucrose.";
RL Nat. Struct. Biol. 5:37-46(1998).
CC -!- FUNCTION: Porin for sucrose uptake.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The C-terminus helps to anchor the porin to the outer membrane.
CC -!- SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family. {ECO:0000305}.
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DR EMBL; M38416; AAA98417.1; -; Genomic_DNA.
DR EMBL; X57400; CAA40656.1; -; Genomic_DNA.
DR PIR; A39127; A39127.
DR PIR; S15193; S15193.
DR PDB; 1A0S; X-ray; 2.40 A; P/Q/R=93-505.
DR PDB; 1A0T; X-ray; 2.40 A; P/Q/R=93-505.
DR PDB; 1OH2; X-ray; 2.40 A; P/Q/R=93-505.
DR PDBsum; 1A0S; -.
DR PDBsum; 1A0T; -.
DR PDBsum; 1OH2; -.
DR AlphaFoldDB; P22340; -.
DR PCDDB; P22340; -.
DR SMR; P22340; -.
DR DrugBank; DB02772; Sucrose.
DR TCDB; 1.B.3.1.2; the sugar porin (sp) family.
DR EvolutionaryTrace; P22340; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0034219; P:carbohydrate transmembrane transport; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR CDD; cd01346; Maltoporin-like; 1.
DR Gene3D; 2.40.170.10; -; 1.
DR InterPro; IPR021570; LamB-type_porin_N_dom.
DR InterPro; IPR003192; Porin_LamB.
DR InterPro; IPR036998; Porin_LamB_sf.
DR Pfam; PF02264; LamB; 1.
DR Pfam; PF11471; Sugarporin_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Membrane; Plasmid; Porin; Signal; Sugar transport;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1846143"
FT CHAIN 23..505
FT /note="Sucrose porin"
FT /id="PRO_0000025187"
FT REGION 44..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 95..108
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 156..167
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 228..239
FT /evidence="ECO:0007829|PDB:1A0S"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 243..255
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 262..275
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 307..321
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 324..338
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 357..389
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 393..406
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 408..425
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 435..451
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 461..471
FT /evidence="ECO:0007829|PDB:1A0S"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:1A0S"
FT STRAND 494..504
FT /evidence="ECO:0007829|PDB:1A0S"
SQ SEQUENCE 505 AA; 55467 MW; DD37733EC22A2135 CRC64;
MYRKSTLAML IALLTSAASA HAQTDISTIE ARLNALEKRL QEAENRAQTA ENRAGAAEKK
VQQLTAQQQK NQNSTQEVAQ RTARLEKKAD DKSGFEFHGY ARSGVIMNDS GASTKSGAYI
TPAGETGGAI GRLGNQADTY VEMNLEHKQT LDNGATTRFK VMVADGQTSY NDWTASTSDL
NVRQAFVELG NLPTFAGPFK GSTLWAGKRF DRDNFDIHWI DSDVVFLAGT GGGIYDVKWN
DGLRSNFSLY GRNFGDIDDS SNSVQNYILT MNHFAGPLQM MVSGLRAKDN DERKDSNGNL
AKGDAANTGV HALLGLHNDS FYGLRDGSSK TALLYGHGLG AEVKGIGSDG ALRPGADTWR
IASYGTTPLS ENWSVAPAML AQRSKDRYAD GDSYQWATFN LRLIQAINQN FALAYEGSYQ
YMDLKPEGYN DRQAVNGSFY KLTFAPTFKV GSIGDFFSRP EIRFYTSWMD WSKKLNNYAS
DDALGSDGFN SGGEWSFGVQ METWF
