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Database: UniProt
Entry: E4THG4_CALNY
LinkDB: E4THG4_CALNY
Original site: E4THG4_CALNY 
ID   E4THG4_CALNY            Unreviewed;       197 AA.
AC   E4THG4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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};
DE   Flags: Precursor;
GN   OrderedLocusNames=Calni_2005 {ECO:0000313|EMBL:ADR19899.1};
OS   Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Calditerrivibrionaceae.
OX   NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR19899.1, ECO:0000313|Proteomes:UP000007039};
RN   [1] {ECO:0000313|EMBL:ADR19899.1, ECO:0000313|Proteomes:UP000007039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC   {ECO:0000313|Proteomes:UP000007039};
RX   PubMed=21475587; DOI=10.4056/sigs.1523807;
RA   Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT   (Yu37-1).";
RL   Stand. Genomic Sci. 4:54-62(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}.
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DR   EMBL; CP002347; ADR19899.1; -; Genomic_DNA.
DR   RefSeq; WP_013452106.1; NC_014758.1.
DR   AlphaFoldDB; E4THG4; -.
DR   STRING; 768670.Calni_2005; -.
DR   MEROPS; S26.025; -.
DR   KEGG; cni:Calni_2005; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_5_1_0; -.
DR   OMA; SDSRFWG; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000007039; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-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; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ADR19899.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007039};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          15..177
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   197 AA;  22981 MW;  676A23138D88198B CRC64;
     MSQEEAVVKK NKFKDTIDSI VVAFVVAMII RAFFIQAYKI PSGSMLNTLL IGDHILVNKV
     AYLFTKPKNG DIIVFEYPLE PEKDFIKRVI AVPGDRIKMV NKKVFLNGKP LNEGYTRYES
     EMVFPEYMNP RDNFEEITIP KGYYFVMGDN RDASFDSRFW GFVPEKSIKG KALIIYWSWN
     FGGKFEFRFN RLLKLIK
//
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