ID A0A0Q9YL56_9COXI Unreviewed; 247 AA.
AC A0A0Q9YL56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=sipP {ECO:0000313|EMBL:KRG17233.1};
GN ORFNames=CC99x_02520 {ECO:0000313|EMBL:KRG17233.1};
OS Candidatus Berkiella cookevillensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG17233.1, ECO:0000313|Proteomes:UP000051494};
RN [1] {ECO:0000313|EMBL:KRG17233.1, ECO:0000313|Proteomes:UP000051494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC99 {ECO:0000313|EMBL:KRG17233.1,
RC ECO:0000313|Proteomes:UP000051494};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG17233.1}.
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DR EMBL; LKHV01000023; KRG17233.1; -; Genomic_DNA.
DR RefSeq; WP_057625602.1; NZ_LKHV02000002.1.
DR AlphaFoldDB; A0A0Q9YL56; -.
DR STRING; 437022.CC99x_02520; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000051494; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:KRG17233.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000051494};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 53..201
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 247 AA; 28700 MW; B51CBEE3F0AD6EEA CRC64;
MLFELLPAVS SALILSLLAL IICLAINIIL FIAKRFQGKK SNYKVPLLKS FCYIFLISFS
IIFPLKYYFG PFRIAHDLMS PNLLRNDIIT IKRPNKNDTF KAGDLILFIF DDPITTYTTR
IIGVAGDVIN FHNGKIWLNG NLLEQPTGQQ MNIDNTTFDV YYESVNNRQY NILKNTIEKN
NSYSQKITVP DGKFFCLLDA RYFYNSAFTT PCLIDEKQIF GYIRNILCSW DSKNNQFRRD
RFFKVPD
//
