ID A0A246JEB6_9BURK Unreviewed; 194 AA.
AC A0A246JEB6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN Name=traF {ECO:0000313|EMBL:OWQ90985.1};
GN ORFNames=CDN99_12600 {ECO:0000313|EMBL:OWQ90985.1};
OS Roseateles aquatilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ90985.1, ECO:0000313|Proteomes:UP000197468};
RN [1] {ECO:0000313|EMBL:OWQ90985.1, ECO:0000313|Proteomes:UP000197468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ90985.1,
RC ECO:0000313|Proteomes:UP000197468};
RX PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT nov., in the class Betaproteobacteria, and emended description of the genus
RT Roseateles.";
RL Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the peptidase S26C family.
CC {ECO:0000256|ARBA:ARBA00005849}.
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:OWQ90985.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIOF01000004; OWQ90985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JEB6; -.
DR OrthoDB; 8524932at2; -.
DR Proteomes; UP000197468; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR014139; Peptidase_S26C_TraF.
DR NCBIfam; TIGR02771; TraF_Ti; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Conjugation {ECO:0000256|ARBA:ARBA00022971};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000197468};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..191
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 194 AA; 21539 MW; E2C9DF2D9C039B52 CRC64;
MSTSSNAAAP RVGLLAWWSR GARLLGYEMR RRWYLFAVLA LIWLLAAMRL FVHHSPMLPV
MVNWTPSIPH HLVYVDYSGL PLARGDLVVY AFEGEAARRD FPGLKDQPFF KRIAGVPGDT
VTVVGREVFV NGVGVGTAKT HTFDRRPLEP IAATVIPPGF LYVQGTSPDS FDSRYRSSGL
VAMRDVTARV KPLL
//
