LSPA_ECOLI
ID LSPA_ECOLI Reviewed; 164 AA.
AC P00804;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:6368552};
DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161}; Synonyms=lsp;
GN OrderedLocusNames=b0027, JW0025;
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 FUNCTION.
RX PubMed=6378662; DOI=10.1016/0014-5793(84)81060-1;
RA Yu F., Yamada H., Daishima K., Mizushima S.;
RT "Nucleotide sequence of the lspA gene, the structural gene for lipoprotein
RT signal peptidase of Escherichia coli.";
RL FEBS Lett. 173:264-268(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=6374664; DOI=10.1073/pnas.81.12.3708;
RA Innis M.A., Tokunaga M., Williams M.E., Loranger J.M., Chang S.-Y.,
RA Chang S., Wu H.C.;
RT "Nucleotide sequence of the Escherichia coli prolipoprotein signal
RT peptidase (lsp) gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3708-3712(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 159-164.
RC STRAIN=K12;
RX PubMed=2011499; DOI=10.1093/nar/19.1.180;
RA Bouvier J., Stragier P.;
RT "Nucleotide sequence of the lsp-dapB interval in Escherichia coli.";
RL Nucleic Acids Res. 19:180-180(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=6368552; DOI=10.1016/s0021-9258(17)43170-x;
RA Tokunaga M., Loranger J.M., Wu H.C.;
RT "Prolipoprotein modification and processing enzymes in Escherichia coli.";
RL J. Biol. Chem. 259:3825-3830(1984).
RN [8]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=1894646; DOI=10.1016/s0021-9258(19)47423-1;
RA Munoa F.J., Miller K.W., Beers R., Graham M., Wu H.C.;
RT "Membrane topology of Escherichia coli prolipoprotein signal peptidase
RT (signal peptidase II).";
RL J. Biol. Chem. 266:17667-17672(1991).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161,
CC ECO:0000269|PubMed:6368552, ECO:0000269|PubMed:6374664,
CC ECO:0000269|PubMed:6378662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of signal peptides from bacterial membrane
CC prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in
CC which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and
CC Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00161,
CC ECO:0000269|PubMed:6368552};
CC -!- ACTIVITY REGULATION: Enzyme activity is inhibited by globomycin, a
CC cyclic peptide antibiotic. {ECO:0000269|PubMed:6368552}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:6368552};
CC Temperature dependence:
CC Optimum temperature is 37-45 degrees Celsius.
CC {ECO:0000269|PubMed:6368552};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00161, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1894646,
CC ECO:0000269|PubMed:6368552}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:1894646,
CC ECO:0000269|PubMed:6368552}.
CC -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC Rule:MF_00161, ECO:0000305}.
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DR EMBL; X00776; CAA25353.1; -; Genomic_DNA.
DR EMBL; K01990; AAA24092.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73138.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96596.1; -; Genomic_DNA.
DR EMBL; X54945; CAA38705.1; -; Genomic_DNA.
DR PIR; C64723; ZPECL.
DR RefSeq; NP_414568.1; NC_000913.3.
DR RefSeq; WP_000083372.1; NZ_LN832404.1.
DR AlphaFoldDB; P00804; -.
DR SMR; P00804; -.
DR BioGRID; 4259402; 214.
DR DIP; DIP-10129N; -.
DR STRING; 511145.b0027; -.
DR MEROPS; A08.001; -.
DR PaxDb; P00804; -.
DR PRIDE; P00804; -.
DR EnsemblBacteria; AAC73138; AAC73138; b0027.
DR EnsemblBacteria; BAB96596; BAB96596; BAB96596.
DR GeneID; 944800; -.
DR KEGG; ecj:JW0025; -.
DR KEGG; eco:b0027; -.
DR PATRIC; fig|1411691.4.peg.2258; -.
DR EchoBASE; EB0543; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_0_6; -.
DR InParanoid; P00804; -.
DR OMA; NRWYFPA; -.
DR PhylomeDB; P00804; -.
DR BioCyc; EcoCyc:EG10548-MON; -.
DR BioCyc; MetaCyc:EG10548-MON; -.
DR UniPathway; UPA00665; -.
DR PRO; PR:P00804; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004175; F:endopeptidase activity; IDA:EcoCyc.
DR GO; GO:0097304; P:lipoprotein biosynthetic process via signal peptide cleavage; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_00161; LspA; 1.
DR InterPro; IPR001872; Peptidase_A8.
DR PANTHER; PTHR33695; PTHR33695; 1.
DR Pfam; PF01252; Peptidase_A8; 1.
DR PRINTS; PR00781; LIPOSIGPTASE.
DR TIGRFAMs; TIGR00077; lspA; 1.
DR PROSITE; PS00855; SPASE_II; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..164
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000178778"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1894646"
FT TRANSMEM 12..26
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1894646"
FT TOPO_DOM 27..69
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1894646"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1894646"
FT TOPO_DOM 89..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1894646"
FT TRANSMEM 96..113
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1894646"
FT TOPO_DOM 114..141
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1894646"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:1894646"
FT TOPO_DOM 160..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:1894646"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 141
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 164 AA; 18156 MW; 65773737DDAA3EB1 CRC64;
MSQSICSTGL RWLWLVVVVL IIDLGSKYLI LQNFALGDTV PLFPSLNLHY ARNYGAAFSF
LADSGGWQRW FFAGIAIGIS VILAVMMYRS KATQKLNNIA YALIIGGALG NLFDRLWHGF
VVDMIDFYVG DWHFATFNLA DTAICVGAAL IVLEGFLPSR AKKQ
