SKP_SALTY
ID SKP_SALTY Reviewed; 161 AA.
AC P0A1Z2; P16974;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperone protein Skp;
DE AltName: Full=Cationic 16 kDa outer membrane protein;
DE AltName: Full=Outer membrane protein OmpH;
DE Flags: Precursor;
GN Name=skp; Synonyms=ompH; OrderedLocusNames=STM0225;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-30.
RX PubMed=2681205; DOI=10.1016/s0021-9258(19)47253-0;
RA Koski P., Rheen M., Kantele J., Vaara M.;
RT "Isolation, cloning, and primary structure of a cationic 16-kDa outer
RT membrane protein of Salmonella typhimurium.";
RL J. Biol. Chem. 264:18973-18981(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2187745; DOI=10.1016/0378-1119(90)90068-3;
RA Koski P., Hirvas L., Vaara M.;
RT "Complete sequence of the ompH gene encoding the 16-kDa cationic outer
RT membrane protein of Salmonella typhimurium.";
RL Gene 88:117-120(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-161.
RX PubMed=2256935; DOI=10.1016/s0006-291x(05)81020-4;
RA Hirvas L., Koski P., Vaara M.;
RT "Primary structure and expression of the Ssc-protein of Salmonella
RT typhimurium.";
RL Biochem. Biophys. Res. Commun. 173:53-59(1990).
RN [5]
RP SIMILARITY TO E.COLI SKP.
RX PubMed=2318304; DOI=10.1016/0014-5793(90)80169-j;
RA Hirvas L., Coleman J., Koski P., Vaara M.;
RT "Bacterial 'histone-like protein I' (HLP-I) is an outer membrane
RT constituent?";
RL FEBS Lett. 262:123-126(1990).
CC -!- FUNCTION: Molecular chaperone that interacts specifically with outer
CC membrane proteins, thus maintaining the solubility of early folding
CC intermediates during passage through the periplasm. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Skp family. {ECO:0000305}.
CC -!- CAUTION: Has been reported to be located in the outer membrane.
CC {ECO:0000305|PubMed:2681205}.
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DR EMBL; J05101; AAA27170.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19189.1; -; Genomic_DNA.
DR PIR; JQ0528; S09104.
DR RefSeq; NP_459230.1; NC_003197.2.
DR RefSeq; WP_000758966.1; NC_003197.2.
DR AlphaFoldDB; P0A1Z2; -.
DR SMR; P0A1Z2; -.
DR STRING; 99287.STM0225; -.
DR PaxDb; P0A1Z2; -.
DR EnsemblBacteria; AAL19189; AAL19189; STM0225.
DR GeneID; 1251743; -.
DR KEGG; stm:STM0225; -.
DR PATRIC; fig|99287.12.peg.238; -.
DR HOGENOM; CLU_101388_2_0_6; -.
DR OMA; EKEQYDM; -.
DR PhylomeDB; P0A1Z2; -.
DR BioCyc; SENT99287:STM0225-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 3.30.910.20; -; 1.
DR InterPro; IPR005632; Chaperone_Skp.
DR InterPro; IPR024930; Skp_dom_sf.
DR PANTHER; PTHR35089; PTHR35089; 1.
DR Pfam; PF03938; OmpH; 1.
DR PIRSF; PIRSF002094; OMP26_Skp; 1.
DR SMART; SM00935; OmpH; 1.
DR SUPFAM; SSF111384; SSF111384; 1.
PE 1: Evidence at protein level;
KW Chaperone; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2681205"
FT CHAIN 21..161
FT /note="Chaperone protein Skp"
FT /id="PRO_0000020178"
FT REGION 97..108
FT /note="Lipopolysaccharide binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 161 AA; 17906 MW; CF04716C1F7A117D CRC64;
MKKWLLAAGL GLAMVTSAQA ADKIAIVNMG NLFQQVAQKT GVSNTLENEF KGRAAELQKM
ETDLQSKMQR LQSMKAGSDR TKLEKDVMSQ RQTFAQKAQA FEKDRARRSN EERNKLVTRI
QTAVKKVAND QSIDLVVDAN TVAYNSSDVK DITADVLKQV K
