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Database: UniProt
Entry: D5BFV1_ZUNPS
LinkDB: D5BFV1_ZUNPS
Original site: D5BFV1_ZUNPS 
ID   D5BFV1_ZUNPS            Unreviewed;       376 AA.
AC   D5BFV1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ADF53064.1};
GN   OrderedLocusNames=ZPR_2742 {ECO:0000313|EMBL:ADF53064.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS   profunda).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53064.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF53064.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA   Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT   to the deep-sea environment and ecological role in sedimentary organic
RT   nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
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DR   EMBL; CP001650; ADF53064.1; -; Genomic_DNA.
DR   RefSeq; WP_013072161.1; NC_014041.1.
DR   AlphaFoldDB; D5BFV1; -.
DR   STRING; 655815.ZPR_2742; -.
DR   KEGG; zpr:ZPR_2742; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_4_5_10; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000001654; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..376
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003069341"
FT   DOMAIN          93..250
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   376 AA;  41814 MW;  A033FE804940684D CRC64;
     MRTNVLYLLV LSFFLVFNQQ LFAAEKPVPT DPFVVVLDAG HGGKDPGNVG NGYREKDIAL
     SIVLKVGKEL ERRGIKVVYT RNTDVFIPLM ERGQIANDAE ADLFVSVHCN SHSSQASGTE
     TFVLGLNRNE TNFEVAKREN SVIYMEEDYK VTYNGFDPNS PESFIGMTLM QEEYLNQSIL
     LADLIQKKFT NDLQRKNRGV KEGALIVLHQ TYMPSVLVEV GFLTNDSEGA FLNSVAGQNK
     MANAIVDGIL GYGNQINLSA IESINQSHPK VPKSASGVSI DGKPADYYEG IIFSVQLAAG
     AKKLETKSYN FKGLNDVFRK KEGKLYKYYL GETSSYLDIQ KVHQKAINKG YRNSYIVAFK
     NGEKITVNEA LKTNLN
//
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