ID A0A1L7I2Z9_9FLAO Unreviewed; 205 AA.
AC A0A1L7I2Z9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Lipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE EC=3.4.23.36 {ECO:0000256|HAMAP-Rule:MF_00161};
DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE AltName: Full=Signal peptidase II {ECO:0000256|HAMAP-Rule:MF_00161};
DE Short=SPase II {ECO:0000256|HAMAP-Rule:MF_00161};
GN Name=lspA {ECO:0000256|HAMAP-Rule:MF_00161};
GN ORFNames=C723_0796 {ECO:0000313|EMBL:OSS40488.1}, GRFL_1263
GN {ECO:0000313|EMBL:APU67987.1};
OS Christiangramia flava JLT2011.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Christiangramia.
OX NCBI_TaxID=1229726 {ECO:0000313|EMBL:APU67987.1, ECO:0000313|Proteomes:UP000186230};
RN [1] {ECO:0000313|EMBL:OSS40488.1, ECO:0000313|Proteomes:UP000194120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2011 {ECO:0000313|EMBL:OSS40488.1,
RC ECO:0000313|Proteomes:UP000194120};
RX PubMed=24048873; DOI=10.1099/ijs.0.051987-0;
RA Liu K., Li S., Jiao N., Tang K.;
RT "Gramella flava sp. nov., a member of the family Flavobacteriaceae isolated
RT from seawater.";
RL Int. J. Syst. Evol. Microbiol. 64:165-168(2014).
RN [2] {ECO:0000313|EMBL:APU67987.1, ECO:0000313|Proteomes:UP000186230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2011 {ECO:0000313|EMBL:APU67987.1,
RC ECO:0000313|Proteomes:UP000186230};
RA Tang K.;
RT "Multi-omics approach to identify versatile polysaccharide utilization
RT systems of a marine flavobacterium Gramella flava.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {ECO:0000256|HAMAP-Rule:MF_00161}.
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:0000256|HAMAP-Rule:MF_00161};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC cleavage). {ECO:0000256|HAMAP-Rule:MF_00161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00161}.
CC -!- SIMILARITY: Belongs to the peptidase A8 family.
CC {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|HAMAP-Rule:MF_00161,
CC ECO:0000256|RuleBase:RU004181}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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DR EMBL; CP016359; APU67987.1; -; Genomic_DNA.
DR EMBL; AMRU01000002; OSS40488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7I2Z9; -.
DR STRING; 1229726.GRFL_1263; -.
DR KEGG; gfl:GRFL_1263; -.
DR OrthoDB; 9810259at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000186230; Chromosome.
DR Proteomes; UP000194120; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_00161; LspA; 1.
DR InterPro; IPR001872; Peptidase_A8.
DR PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR Pfam; PF01252; Peptidase_A8; 1.
DR PRINTS; PR00781; LIPOSIGPTASE.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750, ECO:0000256|HAMAP-
KW Rule:MF_00161};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00161};
KW Lipoprotein {ECO:0000313|EMBL:APU67987.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00161};
KW Reference proteome {ECO:0000313|Proteomes:UP000186230};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 92..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 173..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 144
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 178
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 205 AA; 23000 MW; 3FDC77BA0515BB4F CRC64;
MSLKKAGFII VLILLIDQVS KIYIKTHFAL GNEVEVFDWF RILFVENEGM AWGTKIPGQY
GKLALTLFRL VAIMGIGYWL WDSVKKEGSK TLILSVALIF AGAFGNIIDS VFYGILFSDS
YGHIAEFLPE AGGYGTLFHG KVVDMLYFPI WKGYLPSWIP IWGGEYFTFF EPVFNIADSA
ISVGVAILLI FNKKAFPKNA EEQEA
//