(data stored in ACNUC7421 zone)

SWISSPROT: C3MGM4_SINFN

ID   C3MGM4_SINFN            Unreviewed;       351 AA.
AC   C3MGM4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Putative zinc metalloendopeptidase {ECO:0000313|EMBL:ACP24139.1};
GN   OrderedLocusNames=NGR_c03420 {ECO:0000313|EMBL:ACP24139.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24139.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24139.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24139.1; -; Genomic_DNA.
DR   RefSeq; WP_012706924.1; NC_012587.1.
DR   RefSeq; YP_002824892.1; NC_012587.1.
DR   ProteinModelPortal; C3MGM4; -.
DR   STRING; 394.NGR_c03420; -.
DR   EnsemblBacteria; ACP24139; ACP24139; NGR_c03420.
DR   GeneID; 7791568; -.
DR   KEGG; rhi:NGR_c03420; -.
DR   PATRIC; fig|394.7.peg.3148; -.
DR   eggNOG; ENOG4107X75; Bacteria.
DR   eggNOG; COG0501; LUCA.
DR   HOGENOM; HOG000133185; -.
DR   OMA; EMGHHAY; -.
DR   OrthoDB; POG091H1680; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; C3MGM4.
DR   SWISS-2DPAGE; C3MGM4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM    105    123       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      167    343       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
SQ   SEQUENCE   351 AA;  37609 MW;  0D0A936A3D441D2E CRC64;
     MASDHPAIAV GEWHPAGSSR SVLSGLVEVG DRLIVRDETG ADLAGGRLSL VEISARVGRI
     PRRISFPDGS LFETNDNEAM DRFLAEKGRA GAGIVHRLER FHPRLIAFVA ATILLGVLIY
     RYALPALVEV AIAVTPPIVP RMMSASTLET MDRTLLGESK LDEARRGKIV DGFRRIAAVS
     AAGEAAYTLN FREGGPMGPN AFALPDGTLI LTDELVELAG DDSEMIVGVL AHEIGHVQHK
     HSLRQIYRAA GVAALIMLIA GDIGSGAEDV LVEGGGLLAL SYSRSAEAEA DRHSVELMMK
     AGLDPAAIAR FFELLETKLD DHSDTSIFST HPGTPERRKA ITDLIAELRK N
//

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