ID   A5G9I9_GEOUR            Unreviewed;       163 AA.
AC   A5G9I9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
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   OrderedLocusNames=Gura_4314 {ECO:0000313|EMBL:ABQ28457.1};
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ28457.1, ECO:0000313|Proteomes:UP000006695};
RN   [1] {ECO:0000313|EMBL:ABQ28457.1, ECO:0000313|Proteomes:UP000006695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rf4 {ECO:0000313|EMBL:ABQ28457.1,
RC   ECO:0000313|Proteomes:UP000006695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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 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}.
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; CP000698; ABQ28457.1; -; Genomic_DNA.
DR   RefSeq; WP_011941087.1; NC_009483.1.
DR   AlphaFoldDB; A5G9I9; -.
DR   STRING; 351605.Gura_4314; -.
DR   KEGG; gur:Gura_4314; -.
DR   HOGENOM; CLU_083252_4_0_7; -.
DR   OrthoDB; 9810259at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000006695; 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:UP000006695};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        91..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   TRANSMEM        129..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   163 AA;  18583 MW;  B7F123E40F3EB4E3 CRC64;
     MKLKYLILLT VSILVIGIDQ ATKLFVNKVM DLHSSITVVQ NFFNITYMRN KGAAFSFLSN
     FNYRIPFFIL VSLVAVVVII SVIYKLRPDQ KFAALSLSLI LSGALGNLID RVRLGEVIDF
     LDAHWYEHHW PAFNVADSAI CVGVFLLAID MFLEEQRQKK QKD
//