ID A0A0B7IX38_9PROT Unreviewed; 410 AA.
AC A0A0B7IX38;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=mltA {ECO:0000313|EMBL:CEN56781.1};
GN ORFNames=BN1209_1744 {ECO:0000313|EMBL:CEN56781.1};
OS Candidatus Methylopumilus turicensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN56781.1, ECO:0000313|Proteomes:UP000056322};
RN [1] {ECO:0000313|Proteomes:UP000056322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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};
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DR EMBL; LN794158; CEN56781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7IX38; -.
DR STRING; 1581680.BN1209_1744; -.
DR KEGG; mbac:BN1209_1744; -.
DR HOGENOM; CLU_037751_0_0_4; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000056322; Chromosome 1.
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:UP000056322};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..410
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002133289"
FT DOMAIN 150..307
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 410 AA; 45456 MW; 8E50F290576AC64A CRC64;
MLHKRILRLS FLLISLMMLN ACDRFQVKPT PPVKPDCDCP VQPTPALKPA EVKPEPIKVP
DYGLLKPADW QELDAITKDD VTKAWPAWKL GCASLKAKPA WQAVCNEADK LETPSHESII
DYFKNNFAVY RTTNLDGTNT GLITGYYAPV IKGSRVKTDK YRFPLYTRPD DLITVELSSL
FPELANKRVR GRVVGTKLIP YYNRGEIEAD NSPLKGKEFV WVDDQIDLFF LQIQGSGMVH
FDNGEKMHVG YADQNGQSYQ SIGRLLIEKG ELTADKASMQ GIKDWSRNNP NKLRDLLNAN
PSYVFFRELP PGLPGPIGAL GSPILAERVV AIDPKFVPLG APIFLSTNLP IANKSLNRLM
MAQDTGGAIK GGVRADFYWG AGDAAGKSAG SMKQQGKIWV LLPKDFPLPK
//
