(data stored in SCRATCH zone)

SWISSPROT: C7QHJ5_CATAD

ID   C7QHJ5_CATAD            Unreviewed;       342 AA.
AC   C7QHJ5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   OrderedLocusNames=Caci_0179 {ECO:0000313|EMBL:ACU69134.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69134.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69134.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC       {ECO:0000256|RuleBase:RU362042}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042};
CC       Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; CP001700; ACU69134.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0179; -.
DR   MEROPS; S26.025; -.
DR   EnsemblBacteria; ACU69134; ACU69134; Caci_0179.
DR   KEGG; cai:Caci_0179; -.
DR   eggNOG; ENOG4105C3F; Bacteria.
DR   eggNOG; COG0681; LUCA.
DR   KO; K03100; -.
DR   OMA; FTANEDW; -.
DR   OrthoDB; POG091H023R; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 2.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QHJ5.
DR   SWISS-2DPAGE; C7QHJ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000256|RuleBase:RU362042};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM    132    159       Helical. {ECO:0000256|RuleBase:RU362042}.
FT   DOMAIN      159    202       Peptidase_S24. {ECO:0000259|Pfam:
FT                                PF00717}.
SQ   SEQUENCE   342 AA;  35979 MW;  A47F4DC62A330111 CRC64;
     MAATDPGAPV GSQPAEPPFG DGYGTTGNGY GQQHGFGTEN GYGTENGYGA ENGYGSAPGF
     ASENGYSQDQ GYASEHAFGT QNGYDPVAGD GSAATDPATD PDAADEELAA VPSRGGGRRA
     ARTKAKRRRI PAWLEIVGYV VISLTLTSLI KTFLVQMYYI PSPSMEPTTY KGDRVFVDKL
     SSWVGGAPAR GQVIVFHDPH NWLMSSAGST GGAINLPDVL AAVGILPDQH DDLLIKRIIG
     TGGDTIECKT QDGPVYRNGV ALDESSYIMN GKQGMPCYNG VYKVTVPQGD LWVLGDNREH
     SGDSSWNYLK KGGDAGFVPT KNVVGHVVGV VSWLRDDHPA GS
//

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