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Database: UniProt
Entry: G4NNX1_CHLT4
LinkDB: G4NNX1_CHLT4
Original site: G4NNX1_CHLT4 
ID   G4NNX1_CHLT4            Unreviewed;       628 AA.
AC   G4NNX1; H1ZQD5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=CTO_0022 {ECO:0000313|EMBL:AEP34826.1};
OS   Chlamydia trachomatis serovar A (strain A2497).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=580047 {ECO:0000313|EMBL:AEP34826.1, ECO:0000313|Proteomes:UP000009287};
RN   [1] {ECO:0000313|EMBL:AEP34826.1, ECO:0000313|Proteomes:UP000009287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2497 {ECO:0000313|EMBL:AEP34826.1,
RC   ECO:0000313|Proteomes:UP000009287};
RX   PubMed=21987657; DOI=10.1084/jem.20111266;
RA   Kari L., Whitmire W.M., Olivares-Zavaleta N., Goheen M.M., Taylor L.D.,
RA   Carlson J.H., Sturdevant G.L., Lu C., Bakios L.E., Randall L.B.,
RA   Parnell M.J., Zhong G., Caldwell H.D.;
RT   "A live-attenuated chlamydial vaccine protects against trachoma in nonhuman
RT   primates.";
RL   J. Exp. Med. 208:2217-2223(2011).
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; CP002401; AEP34826.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4NNX1; -.
DR   KEGG; cra:CTO_0022; -.
DR   KEGG; cty:CTR_0201; -.
DR   PATRIC; fig|580047.4.peg.26; -.
DR   Proteomes; UP000009287; 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; 2.
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; 1.
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   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        81..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        601..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          84..201
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          530..581
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   628 AA;  71456 MW;  22CA1F0087E78C6F CRC64;
     MTSSYMSRLY SLNKSRRILH SSFRLLKSTK MLSHPETQKE LQEVLKQLEE AILDQNREDA
     SLFAKQAQAI QKRFPKSKLR ATFDLIYALT FAAILAFLIR QFWFELYEVP TGSMRPTILE
     QDRILVSKTT FGLRLPFSNK SIGYTPEAIT RGELVVFTVG DLPIPSADTK YFGIIPGKKR
     YIKRCMGKPG DTVYFYGGKI YGIDCDGEPI FPQNTENLYH VPYISFDGTP EILTHSEEQT
     DVIFNQFHTP CGKISLPQQA SYGQFFYKNA WHNDTPYALK DPHNEPVSYA DLFGIKNFAI
     VRILTKKQAA LTHVLPSPLS DTYLEIAHTP NVSYPHPHLR PFETQLIPTI EPMKTLLPLR
     KEHIHLIRNN LTTSRFTVVD GYAYKYQPAP MNTSGMARMF ALPMPNIPDG CYEFSKGDVF
     KINMGGFRTK LKQPHPLTQL SNSQVIDLFN CGISFHTIYI PKNPQYAPFP NRYAFFHQGN
     LFVMDSPVFI DSDPALQKFI VSEEEKELQS SEDKPYIAFI DRGPPPESTE EFVSFITNFG
     LKIPEGHVLV LGDNCPMSAD SRDFGFVPVE NLLGSPVGIF WPINRLGLLS SNITPLSLPG
     YLVNGLALGA FLYCIGLWYY RKNHRLFP
//
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