ID I4EZN9_9ACTN Unreviewed; 216 AA.
AC I4EZN9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 ECO:0000313|EMBL:CCH88852.1};
GN OrderedLocusNames=MODMU_3440 {ECO:0000313|EMBL:CCH88852.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88852.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88852.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88852.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC peptides from prolipoproteins. {ECO:0000256|HAMAP-Rule:MF_00161,
CC ECO:0000256|RuleBase:RU000594}.
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 ECO:0000256|RuleBase:RU000594};
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}.
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DR EMBL; FO203431; CCH88852.1; -; Genomic_DNA.
DR AlphaFoldDB; I4EZN9; -.
DR STRING; 477641.MODMU_3440; -.
DR KEGG; mmar:MODMU_3440; -.
DR PATRIC; fig|477641.3.peg.3259; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_2_1_11; -.
DR OMA; PKHFAVF; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000006461; Chromosome.
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 NCBIfam; TIGR00077; lspA; 1.
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.
DR PROSITE; PS00855; SPASE_II; 1.
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:CCH88852.1};
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:UP000006461};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 87..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 175
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 216 AA; 22372 MW; 9144D7DD7622B071 CRC64;
MVGRVPTAIV VPEVADRPHE REGGAVTEQA DQPVRPRRSK ARLLLGLAAA VLALDVGTKL
LVVATLSDRE PLRLLGGAVY LTEARNTGAA FSFAEGATVV FTLIAVVVVV VIVRSARRLF
STGWAVALAL VLGGALGNLV DRVFRDPGFL RGGVVDSISL FDPYGQVWPI FNVADSAIVC
GGVLGAVLAF RGVEFDGGRP GSGREAGATD NAGVGE
//
