ID A0A0B8NBR4_9NOCA Unreviewed; 216 AA.
AC A0A0B8NBR4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:APA97435.1};
GN ORFNames=NS07_v2contig00017-0005 {ECO:0000313|EMBL:GAM45558.1},
GN NS506_03383 {ECO:0000313|EMBL:APA97435.1};
OS Nocardia seriolae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM45558.1, ECO:0000313|Proteomes:UP000019401};
RN [1] {ECO:0000313|EMBL:GAM45558.1, ECO:0000313|Proteomes:UP000019401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N-2927 {ECO:0000313|EMBL:GAM45558.1,
RC ECO:0000313|Proteomes:UP000019401};
RA Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA Oshima S.;
RT "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT quinqueradiata) in Kochi Prefecture, Japan.";
RL Genome Announc. 3:e00082-15(2015).
RN [2] {ECO:0000313|EMBL:APA97435.1, ECO:0000313|Proteomes:UP000180166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM150506 {ECO:0000313|EMBL:APA97435.1,
RC ECO:0000313|Proteomes:UP000180166};
RA Han H.-J.;
RT "Genome sequence of Nocardia seriolae strain EM150506, isolated from
RT Anguila japonica.";
RL Submitted (OCT-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 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; CP017839; APA97435.1; -; Genomic_DNA.
DR EMBL; BAWD02000017; GAM45558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8NBR4; -.
DR STRING; 37332.NS506_03383; -.
DR KEGG; nsr:NS506_03383; -.
DR PATRIC; fig|37332.12.peg.3481; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000019401; Unassembled WGS sequence.
DR Proteomes; UP000180166; 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:GAM45558.1};
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:UP000019401};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 52..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 168..196
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 178
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 216 AA; 22809 MW; 3A319879AA11E53C CRC64;
MGSVSTDRPR ESGAEEPDTA AEPDTSAEES KETAAAQSSE TVAKQPLRLR TLLIIAAVLL
GLDLLTKIIV VATMTPGKPI YLIGDWARLT LVRNPGAAFS MATGMTWLLT LVAAAVVIGV
IRIGRTLRSL PWAIGLGMVL GGALGNLIDR LFRAPGPLQG HVVDFVAVGW WPVFNVADSS
IVCGAVLLVA LTVFGFEPDG TRMHRQHASS AEEKTA
//
