GenomeNet

Database: UniProt
Entry: H1XNJ9_9BACT
LinkDB: H1XNJ9_9BACT
Original site: H1XNJ9_9BACT 
ID   H1XNJ9_9BACT            Unreviewed;       255 AA.
AC   H1XNJ9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   10-APR-2019, entry version 31.
DE   RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU003794};
DE            EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794};
GN   ORFNames=Cabys_2583 {ECO:0000313|EMBL:APF19332.1}, Calab_3639
GN   {ECO:0000313|EMBL:EHO43237.1};
OS   Caldithrix abyssi DSM 13497.
OC   Bacteria; Calditrichaeota; Calditrichae; Calditrichales;
OC   Calditrichaceae; Caldithrix.
OX   NCBI_TaxID=880073 {ECO:0000313|EMBL:EHO43237.1, ECO:0000313|Proteomes:UP000004671};
RN   [1] {ECO:0000313|EMBL:EHO43237.1, ECO:0000313|Proteomes:UP000004671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13497 {ECO:0000313|EMBL:EHO43237.1,
RC   ECO:0000313|Proteomes:UP000004671};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Caldithrix abyssi DSM 13497.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APF19332.1, ECO:0000313|Proteomes:UP000183868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LF13 {ECO:0000313|EMBL:APF19332.1,
RC   ECO:0000313|Proteomes:UP000183868};
RA   Kublanov I., Sigalova O., Gavrilov S., Lebedinsky A., Ivanova N.,
RA   Daum C., Reddy T., Klenk H.P., Goker M., Reva O., Miroshnichenko M.,
RA   Kyprides N., Woyke T., Gelfand M.;
RT   "Genomic analysis of Caldithrix abyssi and proposal of a novel
RT   bacterial phylum Caldithrichaeota.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates
CC       the N-terminal (generally Phe) residue.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-
CC         terminal, basic peptide of 5-8 residues from type IV prepilin,
CC         and then N-methylates the new N-terminal amino group, the methyl
CC         donor being S-adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={ECO:0000256|RuleBase:RU003794};
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|RuleBase:RU003793}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP018099; APF19332.1; -; Genomic_DNA.
DR   EMBL; CM001402; EHO43237.1; -; Genomic_DNA.
DR   RefSeq; WP_006930792.1; NZ_CP018099.1.
DR   STRING; 880073.Calab_3639; -.
DR   EnsemblBacteria; EHO43237; EHO43237; Calab_3639.
DR   KEGG; caby:Cabys_2583; -.
DR   KO; K02654; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; CABY880073:G10QG-3629-MONOMER; -.
DR   BioCyc; GCF_001886815:G1FE4-2407-MONOMER; -.
DR   Proteomes; UP000004671; Chromosome.
DR   Proteomes; UP000183868; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010627; Pept_A24A_N.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   Pfam; PF06750; DiS_P_DiS; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000004671,
KW   ECO:0000313|Proteomes:UP000183868};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004671};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     28       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     96    115       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    127    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    152    171       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    183    216       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       10     93       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      104    211       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   255 AA;  28567 MW;  AE90BE0CB5A91B6B CRC64;
     MKTIDILVIL FGLATGSFLN VCAARLPLKR SVLWGRSQCP VCGHQISWYD NIPLLSFVLL
     KGKCRYCKAK ISLQYPLIEA FSALVTYALY LKFGLSITAV FYGIFIYFLI VIGLIDFKTK
     LILNRLLIPL FTAGVLLNFF GEIIPFKDAL SGAFLGGGIM WMAAILGAKI FKKEAMGMGD
     VKLAFVAGFF LGWQHILLAL YLGFVIALLF ILAIWLFKKK EAPSLIPMGP FLALGFIVYL
     FYGKLLIQWY LSWLS
//
DBGET integrated database retrieval system