(data stored in SCRATCH zone)

SWISSPROT: Q7WAI4_BORPA

ID   Q7WAI4_BORPA            Unreviewed;       257 AA.
AC   Q7WAI4;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   SubName: Full=Putative lipoprotein {ECO:0000313|EMBL:CAE36695.1};
GN   OrderedLocusNames=BPP1393 {ECO:0000313|EMBL:CAE36695.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; BX640427; CAE36695.1; -; Genomic_DNA.
DR   RefSeq; WP_010928014.1; NC_002928.3.
DR   DNASU; 1664767; -.
DR   EnsemblBacteria; CAE36695; CAE36695; BPP1393.
DR   KEGG; bpa:BPP1393; -.
DR   HOGENOM; HOG000264551; -.
DR   KO; K07387; -.
DR   OMA; MDMMTDD; -.
DR   BioCyc; BPAR257311:G1GSY-1432-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WAI4.
DR   SWISS-2DPAGE; Q7WAI4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Hydrolase {ECO:0000256|RuleBase:RU003983};
KW   Lipoprotein {ECO:0000313|EMBL:CAE36695.1};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|RuleBase:RU003983};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU003983}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    257       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004294836.
FT   DOMAIN       94    252       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
SQ   SEQUENCE   257 AA;  27328 MW;  7F45B72F8FD0AB19 CRC64;
     MMKSKTKLLG GALAASLLLA GCASMKSMDT NSLLSAGSDM AKAANLSDAD IIQLSDAACK
     QSDQESKIAP AGNKYSVRLT KLMRGFGNMT LNGQKVNYKV YMTEDVNAWA MGNGCVRVYT
     GLMDLMNDDE LRGVIGHEMG HVALGHTKKA MQTAYAVSAA RQAAGAAGNS VVASLSASQL
     GEMTEKFINA QFSQSQETAA DDFSFDLLTE KKMNRKGLVT AFQKLAELDG GESSMFSSHP
     SSPDRAARME KRLQAGK
//

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