ID J3C3K8_9BURK Unreviewed; 223 AA.
AC J3C3K8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=PMI40_04250 {ECO:0000313|EMBL:EJM97768.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM97768.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJM97768.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJM97768.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:RU362042};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJM97768.1}.
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DR EMBL; AKJA01000134; EJM97768.1; -; Genomic_DNA.
DR RefSeq; WP_008118845.1; NZ_AKJA01000134.1.
DR AlphaFoldDB; J3C3K8; -.
DR STRING; 1144342.PMI40_04250; -.
DR MEROPS; S26.026; -.
DR PATRIC; fig|1144342.3.peg.3874; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000007507; Unassembled WGS sequence.
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; 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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000007507};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..223
FT /note="Signal peptidase I"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003762541"
FT DOMAIN 3..195
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 31
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 223 AA; 24616 MW; 68A1604277D1DC32 CRC64;
MKSLKAWLAF VLMMVALRSA IADYNVVPSG SMMPTVLAGD RILVDKMAFD LRLPLTHIRL
ARLGEPQRGD IVTVDSRQAG ELLLKRVVGL PGDVIALRDN VLTINGAAAR YDPVAVAPAS
GDGVDDARYS DERLDGMSHL VRLAHANPGL RSSYGPVVVP PEHYLMLGDN RDDSADSRYY
GFFARDELMG RTRRIAFSLD SEHGYLPRLE RTGKRLDQGW QTP
//
