ID A0A109RP28_9FLAO Unreviewed; 376 AA.
AC A0A109RP28;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=Lupro_11640 {ECO:0000313|EMBL:AMC11877.1};
OS Lutibacter profundi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC11877.1, ECO:0000313|Proteomes:UP000059672};
RN [1] {ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT "Complete genome sequence of Lutibacter profundus strain LP1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC11877.1, ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|EMBL:AMC11877.1,
RC ECO:0000313|Proteomes:UP000059672};
RX PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT on the Arctic Mid-Ocean Ridge and emended description of the genus
RT Lutibacter.";
RL Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP013355; AMC11877.1; -; Genomic_DNA.
DR RefSeq; WP_068210494.1; NZ_CP013355.1.
DR AlphaFoldDB; A0A109RP28; -.
DR STRING; 1622118.Lupro_11640; -.
DR KEGG; lut:Lupro_11640; -.
DR PATRIC; fig|1622118.3.peg.2393; -.
DR Proteomes; UP000059672; Chromosome.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000059672};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 47..190
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 321..358
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 376 AA; 43901 MW; 4B9E6B0A406FB8C1 CRC64;
MLFISSVLEL LLLITGSIVF IYIYRTGFYI INKIKNNIVR NVVNTCFLLL FILTTIVSIK
LVAFDIYKIP SVSMENTLFP DDIILVDKLK YGARLPRSPY EIPWVNLVFY FNDNGGKRIK
ENWWTYKRIS GLEKIKRGDV FVFNTVSNKY DILVKRCVAL AGDTLNIRNG RIYTNNKLFN
SLDSEKNNYN FKITNKKKIF NIIDSLALNN YISIDNKINY GVANLSKIEL EKLKKTNCID
SITIQIDTFN IDKKLFFNLS KKWTLDNMGP FVIPKKGMKI NLNPETFSLY RGAINSSENY
LIKEIDGIYY INNNKISTYT FKQNYYFMLG DNRKYSIDSR FWGFIPESNI IGKVQCVLFS
NYQSNFQWGR LFKSVN
//