ID A0A097R5P0_HAFAL Unreviewed; 371 AA.
AC A0A097R5P0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 Name=mltA {ECO:0000313|EMBL:AIU74024.1};
GN ORFNames=AT03_17565 {ECO:0000313|EMBL:AIU74024.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74024.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU74024.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74024.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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 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 ECO:0000256|PIRNR:PIRNR019422};
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DR EMBL; CP009706; AIU74024.1; -; Genomic_DNA.
DR RefSeq; WP_025800244.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R5P0; -.
DR GeneID; 78451460; -.
DR KEGG; hav:AT03_17565; -.
DR PATRIC; fig|1453496.5.peg.3611; -.
DR eggNOG; COG2821; Bacteria.
DR HOGENOM; CLU_037751_2_0_6; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000029986; 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; cd22785; DPBB_MltA-like; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PIRNR:PIRNR019422};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422};
KW Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT DOMAIN 125..260
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 371 AA; 41070 MW; D407AE6881A173A4 CRC64;
MKGRWGQYVV GGLLVALLAG CSSRPTDKGQ QYKDGKINDP LELVNRPNAK GKPVNGKDFS
DQLTAIQRAS PSLYNRNTDT FQAVTNWLRA GADTRQLSQF GLNAYQMEGM DNFGNVQFTG
YYTPVIEARY TRQGEFQYPL YRMPSKGKNR RLPERSAIYS GALDNRNLEI GYSNSIMDNF
MMEVQGSGYV DYGDGRPLTF FGYSGKNGHA YRSIGKVLID RGEVAREEMS MQAIRKWADN
HSAAEVRELL EQNPSFVFFK PEMYAPVKGA SGVPLVAKAS VASDRSLIPA GSTLLAEVPL
LDNQGKFTGK YEMRLMVALD VGGAIKGQHF DIYQGIGPEA GHAAGFYNHY GRVWVLKTPQ
SGGPLFSAYN R
//