ID A0A222FQC0_9GAMM Unreviewed; 266 AA.
AC A0A222FQC0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:ASP40990.1};
GN ORFNames=CHH28_18405 {ECO:0000313|EMBL:ASP40990.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP40990.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP40990.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP40990.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-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|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC pass 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; CP022530; ASP40990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FQC0; -.
DR KEGG; bsan:CHH28_18405; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000202440; 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; 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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000202440}.
FT DOMAIN 48..248
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 266 AA; 30200 MW; 77610EB55DEFD10F CRC64;
MDIDFPLVLM VATAVTGIIA AADKLWLGKR RAQQSSHFDE TVKEPFIIEQ SKSFFPVLAL
VFVLRSFVAE PFQIPSGSME PGLVKGDFIL VSKFHYGLRM PVFGNELVSI GMPERGDVMV
FFPPDDPRYF IKRVVGLPGD EIVYRNRQLT INGKEVATEE LGGVPVYNPV RYLAQETLGE
HDADIQWVRA RDMRTSAEVI WAGPEGQWTV PEGHYFMMGD NRGNSADSRS WGFVPERNIV
GKATAVWMHW ESWTDIPSFD RNRWMN
//
