ID   A6GUU9_9BURK            Unreviewed;       432 AA.
AC   A6GUU9;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   03-MAY-2023, entry version 45.
DE   RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE            EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
DE   AltName: Full=Murein hydrolase A {ECO:0000256|ARBA:ARBA00030918};
GN   ORFNames=LMED105_06658 {ECO:0000313|EMBL:EDM82040.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM82040.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM82040.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM82040.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001420};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDM82040.1}.
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DR   EMBL; ABCT01000031; EDM82040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6GUU9; -.
DR   STRING; 391597.LMED105_06658; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000010322; Unassembled WGS sequence.
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-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd14668; mlta_B; 1.
DR   CDD; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.240.50; Barwin-like endoglucanases; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..432
FT                   /note="peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002698133"
FT   DOMAIN          168..324
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   432 AA;  47141 MW;  BA18F605CF00BAB4 CRC64;
     MMNTIRPKAK TISAMSNHMF NPLRCWWPSA VLAALILSGC ATAPTPKTAE CSCPAGEKQV
     QLEKKDEKPA LPLFVKSDFS SLPGWSTANH GRFLEAFAEQ CSVNGNALAK RKATPTGLLE
     ACRKARQNLS GNALLPAQIW MEANFEVWQF QQEDGKKEGL LTGYFEPMLK GSRKAQGAYN
     APLYGVPADL ITVKLDEQYP ELKGKRLRGR LQGNTLVPFF DRAEWERLGP DREKPIVWVD
     DKLDAFLLQV QGSGRVTLPD GSVIRLSYAE QNGHPYKSIG KVLVDRGELT AAQATIPGIR
     NWAKANPGKL DDLLNANPSV VFFKENKVLR PQEGPVGAMG VPLTAQLSLA IDREKVPYGS
     PVWIESSNPV TNAPIAQGTL AQDTGGAIRG RIRADFFWGT GEEAGAAAGL TRQPLKMWLI
     WPKGTPLPES GS
//