ID A0A0Q8EU88_9GAMM Unreviewed; 266 AA.
AC A0A0Q8EU88;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ASD72_11020 {ECO:0000313|EMBL:KRA44513.1};
OS Pseudoxanthomonas sp. Root630.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA44513.1, ECO:0000313|Proteomes:UP000051081};
RN [1] {ECO:0000313|EMBL:KRA44513.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA44513.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA44513.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA44513.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC pass 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KRA44513.1}.
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DR EMBL; LMGY01000016; KRA44513.1; -; Genomic_DNA.
DR RefSeq; WP_056880605.1; NZ_LMGY01000016.1.
DR AlphaFoldDB; A0A0Q8EU88; -.
DR STRING; 1736574.ASD72_11020; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000051081; 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 Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 44..244
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 266 AA; 29522 MW; 32723A6A7BF5B5A2 CRC64;
MVWFETILVV LTLLTGVVWL ADKLFLAKRR KAKGGLLDEE PVLVDYSRAF FPVLAVVLVL
RSFIAEPYKI PSSSMMPNLL IGDFILVNKF SYGLRLPITN QKFLALGEPA RGDVVVFKPP
HDPQNNWIKR VIGLPGDKVG FHGDTVYLNG QPLKYQTLGA YEGTGGNTEA PGATLLREDL
PGRPHTVLEN VGVPPPGGGE GDWIVPPGRY FVMGDNRDNS LDGRFWDYHF LPEENLRGKA
FLIWLNCEGW VCKNGFDASR IGNGIE
//
