(data stored in ACNUC7421 zone)

SWISSPROT: C3MHI0_SINFN

ID   C3MHI0_SINFN            Unreviewed;       417 AA.
AC   C3MHI0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ACP24308.1};
GN   OrderedLocusNames=NGR_c05120 {ECO:0000313|EMBL:ACP24308.1};
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:ACP24308.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24308.1, 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   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|RuleBase:RU004016}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP24308.1; -; Genomic_DNA.
DR   RefSeq; WP_012707093.1; NC_012587.1.
DR   RefSeq; YP_002825061.1; NC_012587.1.
DR   ProteinModelPortal; C3MHI0; -.
DR   STRING; 394.NGR_c05120; -.
DR   EnsemblBacteria; ACP24308; ACP24308; NGR_c05120.
DR   GeneID; 7791738; -.
DR   KEGG; rhi:NGR_c05120; -.
DR   PATRIC; fig|394.7.peg.3324; -.
DR   eggNOG; ENOG4105DZ1; Bacteria.
DR   eggNOG; COG1686; LUCA.
DR   HOGENOM; HOG000141497; -.
DR   KO; K07258; -.
DR   OMA; VYGMIVK; -.
DR   OrthoDB; POG091H04WS; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.1070; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   InterPro; IPR007730; SPOR_dom.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHI0.
DR   SWISS-2DPAGE; C3MHI0.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACP24308.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000313|EMBL:ACP24308.1};
KW   Protease {ECO:0000313|EMBL:ACP24308.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    417       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002929745.
FT   DOMAIN      331    417       SPOR. {ECO:0000259|PROSITE:PS51724}.
SQ   SEQUENCE   417 AA;  44292 MW;  54662BB17E1F8B6B CRC64;
     MRNLQIALAA IVAFVAATAS AFAGSASFVI DARSGRVLSA ENADELNYPA SLTKMMTLYL
     TFEALHRGEI NWQTPVPMSK EAARKPPTKL GLKPGSAITV EEAVYGMIIH SANDAAAAMA
     EKLGGSEAAF AQMMTAKARR LGMTRTVFVN ASGLPASQQV TTARDMAKLG MALLRDFPRE
     YRLFSAQSFN FRGRVVRGHN KLMYRYDGMD GIKTGYTNAS GFNLVSAVRD GNRRVIGVVL
     GGRTAKSRDN KMAALLDQHL GRPSQQGTGT AVAATKPLDT VEVATLPGVS LYAEPKSGQK
     NASAAIMAAS PTRVVPADRP TDLEEVASTQ PKVEAYWQIQ ISTSPSAEAA RKILVEAQSA
     GGAALLGASP HTDVDGSGSA KRYRARFIGF ASREAATSAC NILKKRAYDC QLLPGRS
//

If you have problems or comments...

PBIL Back to PBIL home page