(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y4J7_YERPA

ID   A0A0H2Y4J7_YERPA        Unreviewed;       390 AA.
AC   A0A0H2Y4J7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase A {ECO:0000256|PIRNR:PIRNR019422};
DE            EC=4.2.2.n1 {ECO:0000256|PIRNR:PIRNR019422};
DE   AltName: Full=Murein hydrolase A {ECO:0000256|PIRNR:PIRNR019422};
GN   OrderedLocusNames=YPA_0496 {ECO:0000313|EMBL:ABG12464.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12464.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12464.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12464.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division.
CC       {ECO:0000256|PIRNR:PIRNR019422}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or
CC         the non-reducing ends of the peptidoglycan chains, with
CC         concomitant formation of a 1,6-anhydrobond in the MurNAc
CC         residue.; EC=4.2.2.n1; Evidence={ECO:0000256|PIRNR:PIRNR019422};
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DR   EMBL; CP000308; ABG12464.1; -; Genomic_DNA.
DR   RefSeq; WP_002228046.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12464; ABG12464; YPA_0496.
DR   KEGG; ypa:YPA_0496; -.
DR   KO; K08304; -.
DR   OMA; DQNGHPY; -.
DR   BioCyc; YPES360102:GHZU-519-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   CDD; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR034654; MltA_3D.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; PTHR30124; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H2Y4J7.
DR   SWISS-2DPAGE; A0A0H2Y4J7.
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR019422};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Lyase {ECO:0000256|PIRNR:PIRNR019422}.
FT   DOMAIN      125    259       MltA. {ECO:0000259|SMART:SM00925}.
SQ   SEQUENCE   390 AA;  42914 MW;  4DC72D15FA416447 CRC64;
     MTSRWGKYLL SGIMIAVLAG CQSRPTDRGQ QYKDGRLEQS LELVNEPNAA GKPVNAKDYS
     DQVKVINQSS PGLYNRNSDT FNAVQNWMLA GADTSKLSLF GLNAYQMEGV DNFGNVQFTG
     YYTPVLQARY TPQGEFRHPL YRMPAKGKRR LPDRAAIYAG ALDNRNLIIA YTNSLVDNFM
     MEVQGSGYVD YGDGRPLTFF GYAGKNGHAY RSIGKVLIDR GEVARADMSM QAIRQWAENH
     SEAEVRELLE QNPSFVFFKP VMYAPVKGAS AVPLIAKASV ASDKSLIPPG TTLLAEVPLL
     DDQGKFTGKY QMRLMVALDV GGAIKGQHFD IYQGIGHEAG QAAGFYNHYG RVWVLKNAQS
     SGPLFTAYKG GTQSEPTSND SSLLVNNQDR
//

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