ID A7I255_CAMHC Unreviewed; 278 AA.
AC A7I255;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
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 Name=lepB {ECO:0000313|EMBL:ABS51224.1};
GN OrderedLocusNames=CHAB381_1037 {ECO:0000313|EMBL:ABS51224.1};
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107 {ECO:0000313|EMBL:ABS51224.1, ECO:0000313|Proteomes:UP000002407};
RN [1] {ECO:0000313|Proteomes:UP000002407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A
RC {ECO:0000313|Proteomes:UP000002407};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) 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}; 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; CP000776; ABS51224.1; -; Genomic_DNA.
DR RefSeq; WP_012108893.1; NC_009714.1.
DR AlphaFoldDB; A7I255; -.
DR STRING; 360107.CHAB381_1037; -.
DR KEGG; cha:CHAB381_1037; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_3_7; -.
DR OMA; SDSRFWG; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000002407; 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; 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; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ABS51224.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000002407};
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 DOMAIN 13..246
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 278 AA; 32739 MW; 79DAA7168B96A31A CRC64;
MKILAKLYKF CSSWTGTFII VFIVIFFIAQ AFVIPSGSMK NTLLVGDFLF AKKFVYGIPT
PHIPWLEIPV LPDFNNNGHL IEGNRPKRGE IVIFRNPENT KIHFVKRLFA VGGDEVIFDF
KNMYLRPHEG DDFIDKNYDK KDIVILNGKK FVCEPYKYKG IHYDEKVDMV SATLHYLKIN
KFYMQPLIVS EISQDLTNKI GFNAYYAKIA NDEFFMVGDN RNHSNDSRFW GSVPYKLIVG
KPWFVYFSWN SKKEIRWERI GRFVDTLQND ERFIYEQD
//