ID A0A5C6UB34_9SPHN Unreviewed; 437 AA.
AC A0A5C6UB34;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 13.
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=FSB78_03225 {ECO:0000313|EMBL:TXC70073.1};
OS Sphingomonas ginsenosidivorax.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=862135 {ECO:0000313|EMBL:TXC70073.1, ECO:0000313|Proteomes:UP000321250};
RN [1] {ECO:0000313|EMBL:TXC70073.1, ECO:0000313|Proteomes:UP000321250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHI67 {ECO:0000313|EMBL:TXC70073.1,
RC ECO:0000313|Proteomes:UP000321250};
RX PubMed=23564163; DOI=10.1007/s10482-013-9916-2;
RA Jin X.F., Kim J.K., Liu Q.M., Kang M.S., He D., Jin F.X., Kim S.C.,
RA Im W.T.;
RT "Sphingomonas ginsenosidivorax sp. nov., with the ability to transform
RT ginsenosides.";
RL Antonie Van Leeuwenhoek 103:1359-1367(2013).
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:TXC70073.1}.
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DR EMBL; VOQR01000001; TXC70073.1; -; Genomic_DNA.
DR RefSeq; WP_147083979.1; NZ_VOQR01000001.1.
DR AlphaFoldDB; A0A5C6UB34; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000321250; 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 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000321250}.
FT DOMAIN 172..329
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
FT REGION 23..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 45432 MW; 7F5E277FF184AEAB CRC64;
MRKLGGVALA LMVSACVGGV EPPRTGVAPV GRPPDPVRVH PTRDTGASPN IRGIQSPARI
VGAVPMLAAP VTPAVEPANA VAAGVLPGPA IGSLPITDIQ AEAALAAFVT SCPALQRRVD
QSGLTRGADW QPACAAAASV PRGGARAFFA QWLETVQVGD GRAFATGYYE PEIAGSLTRR
SGYEAPVYGR PDDLIDVDLG AFSTSLKGKK IRGRVQGSNF VPYYDRTAIE QGALANKAPI
LAWARDPVEL FFLQIQGSGR LRLPDGEILR IGYATQNGRD YTGIGALMKA RGLLQPGQTS
MQGIVAWLHD HPVEGQAIMR ENKSFVFFRE LDGAPLGALG LPVIGQVSAA ADVKFVPLGT
PVFLSLDRQD ASGLWVAQDT GGAIKGSNRF DTFWGAGAAA EATAGGMAGR GTAFLLLPVG
TVARLNGARY GGPTPQP
//
