ID A0A1W6YUH3_9BORD Unreviewed; 439 AA.
AC A0A1W6YUH3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CAL12_26085 {ECO:0000313|EMBL:ARP84750.1};
OS Bordetella genomosp. 8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP84750.1, ECO:0000313|Proteomes:UP000194151};
RN [1] {ECO:0000313|EMBL:ARP84750.1, ECO:0000313|Proteomes:UP000194151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU19157 {ECO:0000313|EMBL:ARP84750.1,
RC ECO:0000313|Proteomes:UP000194151};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021108; ARP84750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YUH3; -.
DR STRING; 1416806.CAL12_26085; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000194151; 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-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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 172..332
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 439 AA; 47723 MW; 7EF9B47E271F981E CRC64;
MYRLAPLALL GLILAGCSTV ENGIPPEGAA ATPGESAGAG AATAAETPLV VPSLASLPDS
PTRPLAGRFQ RVSFSDIPAW RDDDLAQFWQ VFLRNCKGLM RPTSGNLTLP ARATPRAWQP
VCAAAIDPAR RPVATDPESV RRFLQTYLQP WRLLAPDGKP ASNMVTGYYE PLVRGSRVQG
GLNQWPLYAP PKDLLTIDLG SIYPELAGKR VRGKLDGKRV VPYDTRAELD NNPARRPPAL
VYVDDPVDNF FLQVQGSGRV LLTDGPDAGK TIRVAYADHN GQPYVSIGRW LVDKGELTAD
QASMQNIRAW AQRNPQRVRE MLNANPAVVF FKEEVVTDPE AGPRGAYGLS LTARRSIAVD
TSFVPLGTPV FLGTTWPGEA RPLDRLVFAQ DTGTAIRGAA RADFYWGYGD AAGQMAGRMK
QRGQMWILWP KQAGEPSAR
//
