SLP_ECOLI
ID SLP_ECOLI Reviewed; 188 AA.
AC P37194; P76709; Q2M7G8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Outer membrane protein Slp;
DE Flags: Precursor;
GN Name=slp; OrderedLocusNames=b3506, JW3474;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-19, AND
RP PALMITOYLATION AT CYS-19.
RC STRAIN=K12;
RX PubMed=8022277; DOI=10.1111/j.1365-2958.1994.tb00383.x;
RA Alexander D.M., St John A.C.;
RT "Characterization of the carbon starvation-inducible and stationary phase-
RT inducible gene slp encoding an outer membrane lipoprotein in Escherichia
RT coli.";
RL Mol. Microbiol. 11:1059-1071(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: The induction of Slp may help to stabilize the outer membrane
CC during carbon starvation and stationary phase.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000269|PubMed:16079137}.
CC -!- INTERACTION:
CC P37194; P37194: slp; NbExp=2; IntAct=EBI-907245, EBI-907245;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16079137}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: Induced upon starvation and slowed growth. cAMP/CRP-
CC independent.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18482.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L23635; AAA60370.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18482.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76531.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77788.1; -; Genomic_DNA.
DR PIR; S47726; S47726.
DR RefSeq; NP_417963.4; NC_000913.3.
DR RefSeq; WP_001350553.1; NZ_LN832404.1.
DR AlphaFoldDB; P37194; -.
DR BioGRID; 4261141; 148.
DR BioGRID; 852330; 1.
DR IntAct; P37194; 4.
DR STRING; 511145.b3506; -.
DR jPOST; P37194; -.
DR PaxDb; P37194; -.
DR PRIDE; P37194; -.
DR EnsemblBacteria; AAC76531; AAC76531; b3506.
DR EnsemblBacteria; BAE77788; BAE77788; BAE77788.
DR GeneID; 948022; -.
DR KEGG; ecj:JW3474; -.
DR KEGG; eco:b3506; -.
DR PATRIC; fig|511145.12.peg.3613; -.
DR EchoBASE; EB1836; -.
DR eggNOG; COG3065; Bacteria.
DR HOGENOM; CLU_100924_0_0_6; -.
DR InParanoid; P37194; -.
DR OMA; FIACRAG; -.
DR PhylomeDB; P37194; -.
DR BioCyc; EcoCyc:EG11890-MON; -.
DR PRO; PR:P37194; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019867; C:outer membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR004658; OMP_Slp.
DR PANTHER; PTHR37530; PTHR37530; 1.
DR Pfam; PF03843; Slp; 1.
DR PIRSF; PIRSF004982; SlP; 1.
DR TIGRFAMs; TIGR00752; slp; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT CHAIN 19..188
FT /note="Outer membrane protein Slp"
FT /id="PRO_0000018187"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:8022277"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:8022277"
SQ SEQUENCE 188 AA; 20964 MW; B2CDBC40E05ADB30 CRC64;
MNMTKGALIL SLSFLLAACS SIPQNIKGNN QPDIQKSFVA VHNQPGLYVG QQARFGGKVI
NVINGKTDTL LEISVLPLDS YAKPDIEANY QGRLLARQSG FLDPVNYRNH FVTILGTIQG
EQPGFINKVP YNFLEVNMQG IQVWHLREVV NTTYNLWDYG YGAFWPEPGW GAPYYTNAVS
QVTPELVK