ID A0A926YF33_9CYAN Unreviewed; 388 AA.
AC A0A926YF33;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
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=H6F73_20680 {ECO:0000313|EMBL:MBD1939701.1};
OS Microcoleus sp. FACHB-68.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Microcoleus.
OX NCBI_TaxID=2692826 {ECO:0000313|EMBL:MBD1939701.1, ECO:0000313|Proteomes:UP000627787};
RN [1] {ECO:0000313|EMBL:MBD1939701.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-68 {ECO:0000313|EMBL:MBD1939701.1};
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:MBD1939701.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-68 {ECO:0000313|EMBL:MBD1939701.1};
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:MBD1939701.1}.
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DR EMBL; JACJOT010000013; MBD1939701.1; -; Genomic_DNA.
DR RefSeq; WP_190760590.1; NZ_JACJOT010000013.1.
DR Proteomes; UP000627787; 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:UP000627787};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..388
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5037318940"
FT DOMAIN 145..286
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 388 AA; 42761 MW; 86959D4A79BACBC3 CRC64;
MIKKLALVLS LGVALSTLPL SVLSSVPLQP IIPDRQNTSN VLGLDDQLWD KAGQPGDRQA
LLTAIDNSLR YLETPAAAKA YQQYPAEDIT LDRVRRSLQR FRQLVIKSNS PAELQAAVRR
EFVYYQSTGS DDRGTVFFTG YYTPQFAASR VPNSVYRYPL YRRPPNFANW SQPHPTRAQL
EGYDGLQAAN GPLRGMELVW LSDRLEAFWV HIQGSAQLQL TDGSVMSVGY GGATNYPYTS
IGRLLANDGK LKLDGQTIPV LTDFFRRNPA EMNNYLPRNN RFIFFAETKA GGPTGSLQVP
VTAERSIATD KSVMPPGALA LVHTKLPYHN AAGQIEQRLV SRYVLDQDAG SAIKGPGRAD
YFVGAGKMAG ERAGVTGTRG NLYYLLLK
//
