ID A0A1I1XDM2_9BACT Unreviewed; 392 AA.
AC A0A1I1XDM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05518672_104290 {ECO:0000313|EMBL:SFE05432.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFE05432.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFE05432.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFE05432.1,
RC ECO:0000313|Proteomes:UP000199596};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOMK01000004; SFE05432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1XDM2; -.
DR STRING; 1884367.SAMN05518672_104290; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000199596; 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 23..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 21..208
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 340..375
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 392 AA; 45576 MW; 1F5B27E4262DF835 CRC64;
MNLAFWKRNK EGQPKKKSAV REWFDAAIFA IIAATLIRTF IFEAYTIPTP SMEKTLLVND
FLFVSKISYG PRIPMTPLAV PFTHHTLPFT KYTKAYSEAV KWKYRRLPGF SDVQRYDVVV
FNFPEGDTVA LEQQEQSYYQ LIRYQTRETV WEQNHVVSRP VDKRENYIKR CMAIAGDTLS
IKDGVVYIDG KQAPIPVESE RKYYVKTNGD QLNPSRLDEL DIDPTPDGTY DSSKFKYNLT
ASAATTLKSW PVVTDLRPFV NPSTQEVNVF PHDTAHYKWT EHNFGPLWIP KKGVTVKLDS
SNVAIYDRII RVYEGNTLEA KNGQFYINNK PADSYTFKMN YYWMMGDNRD NSLDSRYWGF
VPEDHVVGKA WLIWMSYGKG SIRWSRLFKA IK
//
