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Database: UniProt
Entry: A0A109RP28_9FLAO
LinkDB: A0A109RP28_9FLAO
Original site: A0A109RP28_9FLAO 
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
//
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