ID H1LPS3_9PAST Unreviewed; 349 AA.
AC H1LPS3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ORFNames=HMPREF9096_01294 {ECO:0000313|EMBL:EHO47093.1};
OS Haemophilus sp. oral taxon 851 str. F0397.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=762965 {ECO:0000313|EMBL:EHO47093.1, ECO:0000313|Proteomes:UP000005305};
RN [1] {ECO:0000313|EMBL:EHO47093.1, ECO:0000313|Proteomes:UP000005305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0397 {ECO:0000313|EMBL:EHO47093.1,
RC ECO:0000313|Proteomes:UP000005305};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362042}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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:EHO47093.1}.
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DR EMBL; AGRK01000025; EHO47093.1; -; Genomic_DNA.
DR RefSeq; WP_009766811.1; NZ_JH591080.1.
DR AlphaFoldDB; H1LPS3; -.
DR MEROPS; S26.001; -.
DR PATRIC; fig|762965.3.peg.1229; -.
DR HOGENOM; CLU_028723_1_1_6; -.
DR Proteomes; UP000005305; Unassembled WGS sequence.
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};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 86..326
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 349 AA; 39617 MW; C0CF746901A02BE1 CRC64;
MSNLFFVILL AVGFGIWKVL DYFQLPNTFS IVLLILTALS GVLWCYHYFV VTPKRNRKIA
RAEQRSGQVL TDEEKAKIEP ISEASEFLSS LFPVLSVVFL VRSFLFEPFQ IPSGSMESTL
RVGDFLVVNK YAYGVKDPIF QNTIIAGEKP QRGDVIVFKA PQQALIRTGL GATRAAFAEN
LALSSKDNMS GVDYIKRIVG KGGDRVIFDA EQKTLKVVYG KEGKPCEIDC ETKAFEYTQN
PTNPAFPNEL ELTEKGDVTH NVLISEYRRY SGPEFFPQEG MQTAEWLVPE GQYFVMGDHR
DHSDDSRFWG FVPEKNIVGK ATYIWMSLEK EANEWPTGFR FDRFFTAIK
//