ID   A0A5C6TV66_9SPHN        Unreviewed;       400 AA.
AC   A0A5C6TV66;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 14.
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=FRZ32_12250 {ECO:0000313|EMBL:TXC64353.1};
OS   Sphingosinicella ginsenosidimutans.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
OX   NCBI_TaxID=1176539 {ECO:0000313|EMBL:TXC64353.1, ECO:0000313|Proteomes:UP000321249};
RN   [1] {ECO:0000313|EMBL:TXC64353.1, ECO:0000313|Proteomes:UP000321249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS-11 {ECO:0000313|EMBL:TXC64353.1,
RC   ECO:0000313|Proteomes:UP000321249};
RX   PubMed=26115991; DOI=.1007/s12275-015-5087-3;
RA   Kim J.K., Kang M.S., Park S.C., Kim K.M., Choi K., Yoon M.H., Im W.T.;
RT   "Sphingosinicella ginsenosidimutans sp. nov., with ginsenoside converting
RT   activity.";
RL   J. Microbiol. 53:435-441(2015).
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:TXC64353.1}.
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DR   EMBL; VOQQ01000001; TXC64353.1; -; Genomic_DNA.
DR   RefSeq; WP_147043771.1; NZ_BAABIR010000001.1.
DR   AlphaFoldDB; A0A5C6TV66; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000321249; 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   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.
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:UP000321249}.
FT   DOMAIN          142..293
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   400 AA;  42465 MW;  D16690CA4D9BE6E4 CRC64;
     MRGDSIPSRR GPFRGKGLLL QLLMFALASC VAPRRGPPEV TPPPPPPAPA SAIALGVRPG
     PPLPSLDPAR AAAALRSFLV SCPSLVSRAD ASGLATGDDW RPLCGEAASL APGAAAGFFA
     ARFELAEVGD GSAFATGYYE PEIRASRVRQ PGYEVPIYAR PPDLLTADPR TGARGRGRID
     ADGNYVLYYD RGEIEDGALA GRGLEIAWAA DPVELFFLQI QGSGRLRLPD GSLMRIGYAD
     QNGRDYVAIG RLLRERGLIQ GPIGMRQIVD WLHAHPAEGD ALMRENRSYV FFRELTGPGP
     LGALGRPVTP GISVAADPAF VPLGAPVLLQ DMDNPRADGI WIAQDTGGAI RGPNRFDTFW
     GAGPEALETA GSMQSHGRAY ILLPRGRLAR LGRDGSPAQR
//