ID A0A2P9H9H5_PARUW Unreviewed; 636 AA.
AC A0A2P9H9H5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=PC_RS02415 {ECO:0000313|EMBL:SPJ31642.1};
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Protochlamydia.
OX NCBI_TaxID=264201 {ECO:0000313|EMBL:SPJ31642.1, ECO:0000313|Proteomes:UP000000529};
RN [1] {ECO:0000313|EMBL:SPJ31642.1, ECO:0000313|Proteomes:UP000000529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25 {ECO:0000313|EMBL:SPJ31642.1,
RC ECO:0000313|Proteomes:UP000000529};
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; BX908798; SPJ31642.1; -; Genomic_DNA.
DR RefSeq; WP_052278634.1; NC_005861.2.
DR AlphaFoldDB; A0A2P9H9H5; -.
DR STRING; 264201.pc0496; -.
DR KEGG; pcu:PC_RS02415; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000000529; 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; 2.
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; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000000529};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 603..622
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 82..220
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 503..584
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 636 AA; 73682 MW; B41F8B6EBCBD019A CRC64;
MFSKPRPYSL AKSHQILKTS YTFYQKKRKQ LSADHLIHFE TLLESLDKVI QKEDRLKADA
FAKEAEKFTQ IHFKKSFLDY TWEIGLAIFI ALLIAVVVRQ MWFELYEIPT GSMRPTFKEQ
DHLSVTKTAF GLNIPLETNH FYFDPNLVQR TSVVIWSGDG ISHLDSDSTF MTIFPYTKRY
IKRCMGKPGD ILYFYGGKIY GIDQDGNDLK ELRDSPYLSK LDHIPFTNFE GKRAYTQDSQ
LKMINQVAFG HFSLNVGRYR FMRQSIAGEV FNGREWIKDN PLAQKKAHRS IETYSDLWGI
RNIAIARLLT KDQIEKFTTF SLKDFGEGIL YLELRHTPSL SYPLPILSDF YGPSIEGFTT
LIPLEEKHLK ALMDNMYTCR FHVQNEKGVP YRVENQKSPS QHSPSFPNVP NGTYEFYYGK
AQQIHWGGIS TTLPSNHPLY DFTPNNVQKL FNIGIEMNNQ VEPNQAKQAF FPNRYVYFRE
GDLYAMGGKV LDKEDSVLQN FHQTEKNREE KSTEANPYIA FKDYGPPLTS SGELDKEFIR
TFGLKIPQNH YLVLGDNHAM SQDSRFFGPI PQANLQGAPS LILWPPGDRW GFPNQKPYPL
FTFPRLIVWG LASLIGLAWW LFRHHSRTKS VFKKLG
//
