ID A0A427K678_9GAMM Unreviewed; 199 AA.
AC A0A427K678;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 11.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN Name=emtA {ECO:0000313|EMBL:RRZ90446.1};
GN ORFNames=EGK14_13985 {ECO:0000313|EMBL:RRZ90446.1};
OS Erwinia sp. 198.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=2022746 {ECO:0000313|EMBL:RRZ90446.1, ECO:0000313|Proteomes:UP000273595};
RN [1] {ECO:0000313|EMBL:RRZ90446.1, ECO:0000313|Proteomes:UP000273595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=198 {ECO:0000313|EMBL:RRZ90446.1,
RC ECO:0000313|Proteomes:UP000273595};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) 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:RRZ90446.1}.
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DR EMBL; RHUM01000009; RRZ90446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427K678; -.
DR OrthoDB; 5620293at2; -.
DR Proteomes; UP000273595; 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; cd16893; LT_MltC_MltE; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR37423:SF4; ENDO-TYPE MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 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:UP000273595}.
FT DOMAIN 41..162
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 199 AA; 21872 MW; B144796D824FE001 CRC64;
MLLLAGCASQ PHKPNEHQRQ TPLTKAPPGK VAQAWSLFTE NAAHNYGVDQ KLVEAIISVE
SGGNPTVVSK SNAIGLMQIK ASTAGREVYR VQGRRGQPST SELRDPVKNI DIGTAYLKIL
QDSSLSGIRD PKTLRYATIV SYANGAGALL RTFSRDRDRA IAMINAMTPE EFYQHVQNKH
PAAQAPRYLW KVTTAYRTI
//
