(data stored in ACNUC7421 zone)

SWISSPROT: B8IB02_METNO

ID   B8IB02_METNO            Unreviewed;       498 AA.
AC   B8IB02;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:ACL55395.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:ACL55395.1};
GN   OrderedLocusNames=Mnod_0352 {ECO:0000313|EMBL:ACL55395.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55395.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55395.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP001349; ACL55395.1; -; Genomic_DNA.
DR   RefSeq; WP_015927106.1; NC_011894.1.
DR   STRING; 460265.Mnod_0352; -.
DR   EnsemblBacteria; ACL55395; ACL55395; Mnod_0352.
DR   KEGG; mno:Mnod_0352; -.
DR   eggNOG; ENOG4105DZ1; Bacteria.
DR   eggNOG; COG1686; LUCA.
DR   HOGENOM; HOG000141497; -.
DR   KO; K01286; -.
DR   OMA; PRYYRYF; -.
DR   OrthoDB; 1499212at2; -.
DR   BioCyc; MNOD460265:GCZK-353-MONOMER; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF110997; SSF110997; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8IB02.
DR   SWISS-2DPAGE; B8IB02.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACL55395.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Hydrolase {ECO:0000313|EMBL:ACL55395.1};
KW   Protease {ECO:0000313|EMBL:ACL55395.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   DOMAIN      414    498       SPOR. {ECO:0000259|PROSITE:PS51724}.
SQ   SEQUENCE   498 AA;  52787 MW;  203EBE109F189027 CRC64;
     MRGVRGTSGR AVPALIAAAA ILTAMTNPAD ARRRGHHHGG GGGYNPPFAA MVVDVKSGRI
     LHAVNEDALR HPASITKVMT LYLLFEQLER GRMSLDTPLE ISANAARQAP SKLGLRPGAT
     ITVEEAIKAL VTKSANDVAC AIGENIAGSE GAFAEMMTRK AHALGMTRTH YANASGLPDS
     DQITTARDLT ILARAIQDRF PRYYRYFQTR SFAFRGRVIG NHNHLLGRVE GVDGIKTGYT
     RDSGFNLMTS ARINDRHIVA VVLGGKSVAS RDAIMTRLVE ANLPKAYAGA RTTAPVVEVA
     ERPRPAVVAE KPVATRTLVA AADGEDESIE TTASTGRPGQ PLDLNPSRQT ATPSGGRWRS
     GSGLPANAQA YAATPDTSFP APGGKYGSRL PSTEPGEVRA PAPPARTEAP APKPVSVTPW
     VIQLGAMDDE AKAKSMLAEA RQRSGGMLAK AAPFTERVTH GGTTLYRARF SGFSEAESAQ
     DACRALKRNG FTCFATRS
//

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