ID A0A926XI71_9CYAN Unreviewed; 398 AA.
AC A0A926XI71;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
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=H6G60_22875 {ECO:0000313|EMBL:MBD2541626.1};
OS Coleofasciculus sp. FACHB-SPT36.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=2692790 {ECO:0000313|EMBL:MBD2541626.1, ECO:0000313|Proteomes:UP000607678};
RN [1] {ECO:0000313|EMBL:MBD2541626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-SPT36 {ECO:0000313|EMBL:MBD2541626.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD2541626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-SPT36 {ECO:0000313|EMBL:MBD2541626.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) 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:MBD2541626.1}.
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DR EMBL; JACJSL010000097; MBD2541626.1; -; Genomic_DNA.
DR RefSeq; WP_190986894.1; NZ_JACJSL010000097.1.
DR Proteomes; UP000607678; 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:0008933; F:peptidoglycan lytic transglycosylase activity; IEA:TreeGrafter.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:TreeGrafter.
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:UP000607678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..398
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036979113"
FT DOMAIN 154..295
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 398 AA; 43578 MW; 68EABF24A48A5846 CRC64;
MRKTLALLSL SFGVSLGNVT LPALAKDPLS VPLIPVNSNL LNLVCCRSDA LGLDEQIWGQ
NGQAGDRKAL IASIDNSLRY LQTNSAAQAY QQYPVPGITR DRVRRSLVRF RQLVLNSGSA
AELQAAIKRE FVLYQSVGKD NKGNVQYTAY YEPTYTASRK QTAEHRYPLY GMPSNFNSWP
KPHPTRVQLE GEDGLLGANS PLKGLEIAWM SDRLEAFLVQ IQGSAQLQMT DGSVMTVGYA
GGTDYPYTSV GKELAKDGKL PLSGLTLPVL IKYFQQNPLE LSNYIPRNQR FVFFNETNGA
PAMGSVGVPV TPERSIATDK SLMPPGALAL IHTRVPYFNR AGKIEQRLVS RYVLDQDKGS
AILGPGRVDY FIGTGKRAGD RAGVTGGNGQ LYYLLLKQ
//
