ID A0A1V3RKQ2_9BACT Unreviewed; 358 AA.
AC A0A1V3RKQ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=B0E43_04880 {ECO:0000313|EMBL:OOG77438.1};
OS Algoriphagus sp. A40.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1945863 {ECO:0000313|EMBL:OOG77438.1, ECO:0000313|Proteomes:UP000188460};
RN [1] {ECO:0000313|EMBL:OOG77438.1, ECO:0000313|Proteomes:UP000188460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A40 {ECO:0000313|EMBL:OOG77438.1,
RC ECO:0000313|Proteomes:UP000188460};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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}; 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:OOG77438.1}.
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DR EMBL; MUNY01000039; OOG77438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RKQ2; -.
DR STRING; 1945863.B0E43_04880; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000188460; 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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
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; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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 14..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 12..165
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 299..335
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 358 AA; 41131 MW; 763037A0A920A339 CRC64;
MSQTKKKKSA TREWLDALVF AVVAASLIRW LLLEPFTIPT ASMEKSLLVG DFLFVSKMHY
GTRIPKTILQ VPLTHQKIWG TEIPSFSDAI QLPYYRLPGF SDVERNDVVV FNYPVEFQYP
SDLKTNYIKR AVGISGDIIE VKEGELFVNG EASPKPEEMQ YSYDVISNRP LTVDFFAGYG
INAESFMAFS NGSGYMVFGT DQMMETLKSS PVVVSITKRI ESPGVNDSRI FPNGSNYGWN
ADNFGPLQVP AKDWTIDMTA DNVQRYGFTI EKYEGHDQVD MREGELFIDG QKVESYTFKQ
NYYFMMGDNR HDSLDSRFWG FVPEDHIVGK AWFLWLSLDK YESMFNKIRW NRFLKGIN
//
