ID H6SQN9_PARPM Unreviewed; 252 AA.
AC H6SQN9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=RSPPHO_00728 {ECO:0000313|EMBL:CCG07354.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07354.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG07354.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU003993};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; HE663493; CCG07354.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SQN9; -.
DR STRING; 1150469.RSPPHO_00728; -.
DR MEROPS; S26.001; -.
DR KEGG; rpm:RSPPHO_00728; -.
DR PATRIC; fig|1150469.3.peg.839; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_2_5; -.
DR Proteomes; UP000033220; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:CCG07354.1};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000033220};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 18..223
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 252 AA; 28847 MW; 058989644CF4AEF7 CRC64;
MRYESPYMNR KKGGGLGETI KTVAYAFLIA ILIRTFAYEP FRIPSGSMIP TLLVGDYLFV
SKYAYGYSRH SFPFGLIPFE GRVFGSAPQR GDVVVFKEPS DTSVDFIKRV VGLPGDRIQV
LNGILHVNGE PVRRERMEDY VRRDPSGSVL RQTRYLETLP EGLSHPILEI HGDDYFLDNT
RVFLVPEGHY FMMGDNRDSS QDSRTSVGFV PAENLVGRAE FLFFSHDGSA ALWEPWKWPH
AIRWDRFFQA IH
//
