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Database: UniProt
Entry: A0A077FK22_9RICK
LinkDB: A0A077FK22_9RICK
Original site: A0A077FK22_9RICK 
ID   A0A077FK22_9RICK        Unreviewed;       258 AA.
AC   A0A077FK22;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   Name=lepB {ECO:0000313|EMBL:AIL64885.1};
GN   ORFNames=NOVO_02455 {ECO:0000313|EMBL:AIL64885.1};
OS   Rickettsiales bacterium Ac37b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL64885.1, ECO:0000313|Proteomes:UP000028936};
RN   [1] {ECO:0000313|EMBL:AIL64885.1, ECO:0000313|Proteomes:UP000028936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac37b {ECO:0000313|EMBL:AIL64885.1,
RC   ECO:0000313|Proteomes:UP000028936};
RA   Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.;
RT   "Genome sequence of a novel Rickettsiales species cultured from Amblyomma
RT   cajennense.";
RL   Submitted (JAN-2015) 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:RU003993};
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; CP009217; AIL64885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077FK22; -.
DR   STRING; 1528098.NOVO_02455; -.
DR   KEGG; rbt:NOVO_02455; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   Proteomes; UP000028936; 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; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
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; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:AIL64885.1};
KW   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028936};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          11..215
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   258 AA;  29613 MW;  CC312EF39327E6F6 CRC64;
     MLKRDKAYYG EFFRTFLVAI IVALVFRSFV YEPYHVPSGS MKPTLIDGDY IFVSKFSYGY
     SRYSLPLGLN LFAGRVAEFA HPERGDVIVF RNPYHPSVNY IKRLIGLPGD KIQVMNGVVY
     INGVAVEQIR EGTFIDGNGK HIEKYVEVLP NGVSYNVLKD KERGPLDNTK IYTVPKDKYF
     FMGDNRDNSI DSRFLDKVGY VPYVNIVGKA QLIFFSSKSS LWAIWTWLYD LNLDRFFTKL
     APKQVVGNNF ESITDRAN
//
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