ID A0A0F0VCN7_PLUGE Unreviewed; 454 AA.
AC A0A0F0VCN7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN Name=mltD {ECO:0000313|EMBL:KMK11172.1};
GN ORFNames=ABW06_22960 {ECO:0000313|EMBL:KMK11172.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK11172.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK11172.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK11172.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) 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 -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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:KMK11172.1}.
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DR EMBL; LDZF01000033; KMK11172.1; -; Genomic_DNA.
DR RefSeq; WP_045290701.1; NZ_VWRP01000071.1.
DR AlphaFoldDB; A0A0F0VCN7; -.
DR STRING; 61647.LG71_24025; -.
DR PATRIC; fig|61647.13.peg.3531; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR Proteomes; UP000036196; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 2.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000036196}.
SQ SEQUENCE 454 AA; 49423 MW; F5A5FD188AD28E57 CRC64;
MKARAIIFAS VLLAGCQANH GGSVQQHAQS LSAASQGEAG KFASHSRWMD DGTSFAQDQD
LWASISDELK MGIPDNARIR EQKQKYLRNK SYLHDVTVRA EPYMYWIAGQ VKKRNMPMEL
VLLPIVESAF DPHATSGANA AGIWQIIPST GRNYGLKQTR SYDARRDVVA STTAALNMMQ
RLNKMFDGDW LLTVAAYNSG EGRVMKAVKA NKARGKPADF WSLSLPYETK IYVPKMLALS
DILKNSKRYG VQLPTADESR ALARVRLDNP VELSQVADMA GMSITRLKAF NAGVKGSTLG
ASGPKYVMVP KKHADQLRES LASGDIAAVQ PTLVADNTPL TSRSYRVRSG DTLSGIASRL
GVSTSDLKQW NNLRGSGLKI GQSLTVGAGS SAARLAKNSD SITYRVRKGD SLSSIAKSHG
INIKDLVRWN SDTDNLKPGD RLTLFVSNSD RPDS
//
