ID A0A2N5ENP5_9GAMM Unreviewed; 460 AA.
AC A0A2N5ENP5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN ORFNames=CYR34_08725 {ECO:0000313|EMBL:PLR50584.1};
OS Chimaeribacter arupi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chimaeribacter.
OX NCBI_TaxID=2060066 {ECO:0000313|EMBL:PLR50584.1, ECO:0000313|Proteomes:UP000234626};
RN [1] {ECO:0000313|EMBL:PLR50584.1, ECO:0000313|Proteomes:UP000234626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2016Iso1 {ECO:0000313|EMBL:PLR50584.1,
RC ECO:0000313|Proteomes:UP000234626};
RA Rossi A., Fisher M.;
RT "Characterization of six clinical isolates of Enterochimera gen. nov., a
RT novel genus of the Yersiniaciae family and the three species Enterochimera
RT arupensis sp. nov., Enterochimera coloradensis sp. nov, and Enterochimera
RT californica sp. nov.";
RL Submitted (DEC-2017) 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:PLR50584.1}.
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DR EMBL; PJZK01000007; PLR50584.1; -; Genomic_DNA.
DR RefSeq; WP_072930078.1; NZ_PJZK01000007.1.
DR AlphaFoldDB; A0A2N5ENP5; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000234626; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-KW.
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 outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000234626};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..460
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014982483"
FT DOMAIN 350..394
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 408..458
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 50634 MW; FB1FAF4E17E05BDC CRC64;
MKAKAILLAS VLLVGCQASR HDATPPLQHA QSLSSAGQSE AGEYTGAGRE TTARWLGSSN
SDIAQQEDLW NFISDELKME VPENSRIREQ KKRYLKQKSY LHDVTLRAEP YMYWIVEQIK
QRKMPMELVL LPIVESAFDP KATSSANAAG LWQIVPSTGR TYGLKQNQWY DGRRDVVAST
TAALDMMQRL NRMFDGDWLL TVAAYNSGEG RVLQAIKANK AQGRPTNFWA LALPRETSIY
VPKMLALSDI LKHSKQYGIR LPKTNENRAL ARVEVGQQMQ LTQAAEMAGM SLTKLKSFNT
GYKKGVTAPN GPHYILVPKA HADQLKDSLA DSDIAAVETK LAKNSAASGS SYTVRPGDTL
SAIAARLNVK TSDLQRWNNL GRSSTVKVGQ NLQIADKASA NLTAANSITY QVRKGDSLAS
IARRHGVNIS DVMRWNSASN NLQPGDKLTL FVNNKLTPDT
//
