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Database: UniProt
Entry: H1LPS3_9PAST
LinkDB: H1LPS3_9PAST
Original site: H1LPS3_9PAST 
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
//
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