(data stored in ACNUC7421 zone)

HOGENOM: MARMM_1_PE1002

ID   MARMM_1_PE1002                       STANDARD;      PRT;   467 AA.
AC   MARMM_1_PE1002; Q0AQY9;
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=Membrane-bound lytic murein transglycosylase F; EC=4.2.2
DE   n1;AltName: Full=Murein lyase F;Flags: Precursor; (MARMM_1.PE1002).
GN   Name=mltF; OrderedLocusNames=Mmar10_1005;
OS   MARICAULIS MARIS MCS10.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MARMM_1.PE1002.
CC       Maricaulis maris MCS10, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:MLTF_MARMM
CC   -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan
CC       strands and insoluble, high-molecular weight murein sacculi, with
CC       the concomitant formation of a 1,6-anhydromuramoyl product. Lytic
CC       transglycosylases (LTs) play an integral role in the metabolism of
CC       the peptidoglycan (PG) sacculus. Their lytic action creates space
CC       within the PG sacculus to allow for its expansion as well as for
CC       the insertion of various structures such as secretion systems and
CC       flagella (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exolytic cleavage of the (1->4)-beta-
CC       glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-
CC       acetylglucosamine (GlcNAc) residues in peptidoglycan, from either
CC       the reducing or the non-reducing ends of the peptidoglycan chains,
CC       with concomitant formation of a 1,6-anhydrobond in the MurNAc
CC       residue.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane
CC       protein. Note=Attached to the inner leaflet of the outer membrane
CC       (By similarity).
CC   -!- DOMAIN: The N-terminal domain does not have lytic activity and
CC       probably modulates enzymatic activity. The C-terminal domain is
CC       the catalytic active domain (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC       solute-binding protein 3 family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       transglycosylase slt family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI65298.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000218316 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0AQY9; -.
DR   EMBL; CP000449; ABI65298.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_756236.1; NC_008347.1.
DR   ProteinModelPortal; Q0AQY9; -.
DR   STRING; Q0AQY9; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   GeneID; 4284345; -.
DR   GenomeReviews; CP000449_GR; Mmar10_1005.
DR   KEGG; mmr:Mmar10_1005; -.
DR   NMPDR; fig|394221.5.peg.982; -.
DR   eggNOG; COG4623; -.
DR   ProtClustDB; PRK10859; -.
DR   BioCyc; MMAR394221:MMAR10_1005-MON; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
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:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   HAMAP; MF_02016; MltF; 1; -.
DR   InterPro; IPR023346; Lysozyme-like_dom.
DR   InterPro; IPR008258; Lytic_TGlycosylase-like_cat.
DR   InterPro; IPR023703; MltF.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; FALSE_NEG.
DR   HOGENOMDNA; MARMM_1.PE1002; -.
KW   putative transglycosylase;
KW   Cell membrane; Cell outer membrane; Cell wall biogenesis/degradation;
KW   Complete proteome; Lyase; Membrane; Signal.
SQ   SEQUENCE   467 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQTLRALVA TLKTWPSRAV SLLLLALALP VGCSEPPPPV RDPDTLATIR ERGELVVLTL
     AGPTSLIENE DGPPSGYEVD LANAFAASLG VTARFEVAAS LPDLFDALAA GDGHVAAAGL
     TLTPERSERL AFSPVYKSVT EQLVCRRGGV NPTRLERLPD ADIVVLEGSS YEETLRAIGV
     THTALRWRTR PGGSAMPLLE AVDDGQADCT IADSHLADFA RRRHPELIVA RNLTGEQPLA
     WAYDARIDGL GEALSAWFAT AHADGLLEAL DETWFGRFGD YDYVDVARFV RRVENRLPRY
     RRLFEAAADE LPFEWELLAA QAYQESHWDP DAVSATGVRG LMMLTLSTAE RVGIDDRTDP
     EQSIVGGAAY LDDLYERVPD SVTGPDRLWF ALAAYNVGMG HMYDARRLAE RLGRDKDSWD
     DLAEILPLLS DPAHYSTLRY GYARGHEPVR YVAKIREYRA LLAAQDL
//

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