SYDP_ECOLI
ID SYDP_ECOLI Reviewed; 181 AA.
AC P0A8U0; P43526; Q2MA41;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein Syd;
GN Name=syd; Synonyms=ydr; OrderedLocusNames=b2793, JW2764;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16.
RC STRAIN=K12;
RX PubMed=7890670; DOI=10.1074/jbc.270.10.5519;
RA Shimoike T., Taura T., Kihara A., Yoshihisa T., Akiyama Y., Cannon K.,
RA Ito K.;
RT "Product of a new gene, syd, functionally interacts with SecY when
RT overproduced in Escherichia coli.";
RL J. Biol. Chem. 270:5519-5526(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INTERACTION WITH SECY.
RC STRAIN=K12;
RX PubMed=9668058; DOI=10.1074/jbc.273.30.18835;
RA Matsuo E., Mori H., Shimoike T., Ito K.;
RT "Syd, a SecY-interacting protein, excludes SecA from the SecYE complex with
RT an altered SecY24 subunit.";
RL J. Biol. Chem. 273:18835-18840(1998).
CC -!- FUNCTION: Interacts with the SecY protein in vivo. May bind
CC preferentially to an uncomplexed state of SecY, thus functioning either
CC as a chelating agent for excess SecY in the cell or as a regulatory
CC factor that negatively controls the translocase function.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Loosely associated with the cytoplasmic side of
CC the inner membrane, probably via SecY.
CC -!- SIMILARITY: Belongs to the Syd family. {ECO:0000305}.
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DR EMBL; D38520; BAA07525.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40443.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75835.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76865.1; -; Genomic_DNA.
DR PIR; A55944; A55944.
DR RefSeq; NP_417273.1; NC_000913.3.
DR RefSeq; WP_000342431.1; NZ_STEB01000030.1.
DR PDB; 3FFV; X-ray; 2.00 A; A/B=1-181.
DR PDBsum; 3FFV; -.
DR AlphaFoldDB; P0A8U0; -.
DR SMR; P0A8U0; -.
DR BioGRID; 4263497; 21.
DR DIP; DIP-48106N; -.
DR STRING; 511145.b2793; -.
DR jPOST; P0A8U0; -.
DR PaxDb; P0A8U0; -.
DR PRIDE; P0A8U0; -.
DR EnsemblBacteria; AAC75835; AAC75835; b2793.
DR EnsemblBacteria; BAE76865; BAE76865; BAE76865.
DR GeneID; 58390453; -.
DR GeneID; 947271; -.
DR KEGG; ecj:JW2764; -.
DR KEGG; eco:b2793; -.
DR PATRIC; fig|1411691.4.peg.3940; -.
DR EchoBASE; EB2792; -.
DR eggNOG; ENOG502ZCMR; Bacteria.
DR HOGENOM; CLU_121866_0_0_6; -.
DR OMA; GIPSPCI; -.
DR PhylomeDB; P0A8U0; -.
DR BioCyc; EcoCyc:G7451-MON; -.
DR EvolutionaryTrace; P0A8U0; -.
DR PRO; PR:P0A8U0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IDA:EcoCyc.
DR CDD; cd16323; Syd; 1.
DR Gene3D; 3.40.1580.20; -; 1.
DR HAMAP; MF_01104; Syd; 1.
DR InterPro; IPR009948; Syd.
DR InterPro; IPR038228; Syd_sf.
DR Pfam; PF07348; Syd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome.
FT CHAIN 1..181
FT /note="Protein Syd"
FT /id="PRO_0000214136"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3FFV"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3FFV"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:3FFV"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3FFV"
FT HELIX 106..125
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3FFV"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3FFV"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3FFV"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:3FFV"
SQ SEQUENCE 181 AA; 20708 MW; 95F6490B168DC222 CRC64;
MDDLTAQALK DFTARYCDAW HEEHKSWPLS EELYGVPSPC IISTTEDAVY WQPQPFTGEQ
NVNAVERAFD IVIQPTIHTF YTTQFAGDMH AQFGDIKLTL LQTWSEDDFR RVQENLIGHL
VTQKRLKLPP TLFIATLEEE LEVISVCNLS GEVCKETLGT RKRTHLASNL AEFLNQLKPL
L
