ID C1DXT6_SULAA Unreviewed; 164 AA.
AC C1DXT6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
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:ACN99395.1};
GN OrderedLocusNames=SULAZ_0201 {ECO:0000313|EMBL:ACN99395.1};
OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium.
OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN99395.1, ECO:0000313|Proteomes:UP000001369};
RN [1] {ECO:0000313|EMBL:ACN99395.1, ECO:0000313|Proteomes:UP000001369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC {ECO:0000313|Proteomes:UP000001369};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC 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; CP001229; ACN99395.1; -; Genomic_DNA.
DR RefSeq; WP_012674713.1; NC_012438.1.
DR AlphaFoldDB; C1DXT6; -.
DR STRING; 204536.SULAZ_0201; -.
DR KEGG; saf:SULAZ_0201; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_3_0; -.
DR OrthoDB; 9810259at2; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000001369; 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}; Cell inner membrane {ECO:0000256|HAMAP-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 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:UP000001369};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 121
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ SEQUENCE 164 AA; 18610 MW; DA32B3B1E1603AC8 CRC64;
MNKKSVAFWG VFFLVFFLDL ITKYLAETLL LDRTVSVIPN FFDLTLVWNK GAAFGMLAEA
PEYVRKFILV GSSIVAIIVS VVYFLKSKDK LSNLEIISLA LIGGGSLGNL YDRFFLGQVR
DFLDFYIKDH HWPAFNIADA SITVGIGLFI FYELHLKKRS IINN
//
