(data stored in SCRATCH zone)

HOGENOM: SAENT4_1_PE1006

ID   SAENT4_1_PE1006                      STANDARD;      PRT;   203 AA.
AC   SAENT4_1_PE1006; Q5PN08;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Endo-type membrane-bound lytic murein transglycosylase A;
DE   EC=4.2.2 n2;AltName: Full=Peptidoglycan lytic endotransglycosylase;Flags:
DE   Precursor; (SAENT4_1.PE1006).
GN   Name=emtA; Synonyms=mltE; OrderedLocusNames=SPA1074;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR PARATYPHI A STR. ATCC 9150.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SAENT4_1.PE1006.
CC       Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:EMTA_SALPA
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division.
CC       Preferentially cleaves at a distance of more than two disaccharide
CC       units from the ends of the glycan chain (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endolytic cleavage of the (1->4)-beta-
CC       glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-
CC       acetylglucosamine (GlcNAc) residues in peptidoglycan with
CC       concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the transglycosylase slt family.
CC   -!- GENE_FAMILY: HOG000219318 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5PN08; -.
DR   EMBL; CP000026; AAV77045.1; -; Genomic_DNA.
DR   RefSeq; YP_150357.1; NC_006511.1.
DR   ProteinModelPortal; Q5PN08; -.
DR   PRIDE; Q5PN08; -.
DR   GeneID; 3177940; -.
DR   GenomeReviews; CP000026_GR; SPA1074.
DR   KEGG; spt:SPA1074; -.
DR   OMA; PWNPEVP; -.
DR   ProtClustDB; PRK15470; -.
DR   BioCyc; SENT295319:SPA1074-MON; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:EC.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   HAMAP; MF_01381; EmtA; 1; -.
DR   InterPro; IPR023946; EmtA.
DR   InterPro; IPR023346; Lysozyme-like_dom.
DR   InterPro; IPR008258; Lytic_TGlycosylase-like_cat.
DR   InterPro; IPR000189; Transglyc_AS.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
DR   HOGENOMDNA; SAENT4_1.PE1006; -.
KW   membrane-bound lytic murein transglycosylase E;
KW   Cell membrane; Cell outer membrane; Cell wall biogenesis/degradation;
KW   Complete proteome; Lipoprotein; Lyase; Membrane; Palmitate; Signal.
SQ   SEQUENCE   203 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKLRWFAFLV VILAGCSSKQ DYRNPPWNAE VPVKRAMQWM PISEKAGAAW GVDPHLITAI
     IAIESGGNPN AVSKSNAIGL MQLKASTSGR DVYRRMGWRG EPTTSELKNP ERNISMGAAY
     LSILENGPLA GIKDPQVMQY ALVVSYANGA GALLRTFSSD RKKAIEKIND LDADEFFEHV
     VDNHPAPQAP RYIWKLQQAL DAM
//

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