ID A0A238X107_9FLAO Unreviewed; 514 AA.
AC A0A238X107;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=SAMN06265371_104264 {ECO:0000313|EMBL:SNR52308.1};
OS Lutibacter agarilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR52308.1, ECO:0000313|Proteomes:UP000198384};
RN [1] {ECO:0000313|EMBL:SNR52308.1, ECO:0000313|Proteomes:UP000198384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR52308.1,
RC ECO:0000313|Proteomes:UP000198384};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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|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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; FZNT01000004; SNR52308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238X107; -.
DR Proteomes; UP000198384; 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; IPR043739; DUF5684.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
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; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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 Reference proteome {ECO:0000313|Proteomes:UP000198384};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 489..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 125..311
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 416..458
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 253
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 514 AA; 59625 MW; 60943A8AFA4B5664 CRC64;
MMTITELFIA FLILQLIHFA GTWKLYSKAG RKPWEAIVPI YNAIVLMKII NRPTWWVILL
FIPVINLLMF PIVWIETARS FGRNSNIDTI LAVVTLGFYN FYLNYVADVT YIEDRSLKPR
TELGEWVSSI AFAIIAATLV HTYVMQPYTI PTSSLEKSLL IGDFLFVSKF HYGARVPMTP
IAAPMVHDSL PFVGTKSYLQ KPQLPYMRVP GFQHIKRNEI VVFSWPVDTV QRFFDKSNIH
IQKPIDKKSN YVKRCVGIAG DSLEIRNGYI YINGEKTVLP DRAKTQYYHK VETEGQQLSG
TMLKRYNITE GQNMGNFYYL NLTDENAAKL AKNPLIKSVT KEIEPSGNYD ASVFPHDSRY
PWSKDNFGPI YIPEEGKTVE LNAASLPFYK RIIEEYEHNQ LTVNGDEIYI NGKLATSYTF
KQNYYWMMGD NRHNSEDARY WGYVPFDHVV GKPVFIWFSW DTNGQGISNK IRWERLFTTV
HGNGKPVSYL YYFLAALALW YGVSIYRKRR KENK
//
