ID E8QVS1_HELPW Unreviewed; 290 AA.
AC E8QVS1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 OrderedLocusNames=HPSA_02665 {ECO:0000313|EMBL:ADU84542.1};
OS Helicobacter pylori (strain SouthAfrica7).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907239 {ECO:0000313|EMBL:ADU84542.1, ECO:0000313|Proteomes:UP000007467};
RN [1] {ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|Proteomes:UP000007467};
RA Kersulyte D., Segal I., Mistry R., Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain SouthAfrica7.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU84542.1, ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|EMBL:ADU84542.1,
RC ECO:0000313|Proteomes:UP000007467};
RX PubMed=24072860;
RA Duncan S.S., Bertoli M.T., Kersulyte D., Valk P.L., Tamma S., Segal I.,
RA McClain M.S., Cover T.L., Berg D.E.;
RT "Genome Sequences of Three hpAfrica2 Strains of Helicobacter pylori.";
RL Genome Announc. 1:e00729-13(2013).
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; CP002336; ADU84542.1; -; Genomic_DNA.
DR RefSeq; WP_000670719.1; NC_017361.1.
DR AlphaFoldDB; E8QVS1; -.
DR KEGG; hes:HPSA_02665; -.
DR PATRIC; fig|907239.3.peg.541; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_3_7; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000007467; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 12..244
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 290 AA; 33725 MW; 9EAE5C3FCC2E7E4B CRC64;
MKFLRSVYAF CSSWVGTIVI VLLVIFFIAQ AFIIPSRSMV GTLYEGDMLF VKKFSYGIPI
PKIPWIELPV MPDFKNNGHL IEGTRPKRGE VVVFIPPHEK KSYYVKRNFA VGGDEVLFTS
EGFYLHPFES DTDKNYISKH YPNAMTKEFM GKIFVLNPYK NKHPGIHYQK DNETFHFMEQ
LATQGAEANI SMQLIQIEGE KVFYKKINND EFFMIGDNRD NSSDSRFWGS VAYKNIVGSP
WFVYFSLSLK NSLEVDAENN PKKRYLVRWE RMFKSVEGLE KIIKKENATH
//