ID A0A0V7ZSL0_9CYAN Unreviewed; 425 AA.
AC A0A0V7ZSL0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BC008_27405 {ECO:0000313|EMBL:KST66920.1}, BC008_28770
GN {ECO:0000313|EMBL:KST67190.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST67190.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST67190.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST67190.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
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:KST67190.1}.
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; LMTZ01000092; KST66920.1; -; Genomic_DNA.
DR EMBL; LMTZ01000090; KST67190.1; -; Genomic_DNA.
DR RefSeq; WP_027845788.1; NZ_LMTZ01000092.1.
DR AlphaFoldDB; A0A0V7ZSL0; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000053372; 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:UP000053372}.
FT DOMAIN 181..322
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
FT REGION 36..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47947 MW; 60091B5864402024 CRC64;
MKKMFALVSL SLGITLVTPV FSASAQVRLP RRLPRSLPVP SQSQELSPQI PSKLETPPPA
LKPMDMDFEC SPRHACLGWD SQLFWGRFGK TADRWSMVRS IDHSLRYLKT PTAARVYADY
PIEGITLERV RRSLLRFRQL LLKSKTPTQL QDAVRREFEF YKSIGNDGQG TVKFTSYYEP
IYEASRQRTS VYKYPLYRLP PDFAQWPQPH PKRLELEGKD GLLGDKSPLK GLELFWFRNR
LDAYLIHIQG SAKLKLTDGT TTSVGYANGT QYPWTSIGKE LLKDERITRK SASMPGILRH
FKLNPEDMNE YLPRWERFIF FRDKGNTPAV GSIGVPVTAD RSIATDKSIM PPGALAIINS
SFPYPTKGGG LTYRRVSRFV LDQDTGSAIK GPGRVDYFAG RGKIAGDRAG VTGGPGTLYY
LLLKK
//
