ID   A0A246K2Y6_9SPHN        Unreviewed;       434 AA.
AC   A0A246K2Y6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=CDQ92_04350 {ECO:0000313|EMBL:OWQ99836.1};
OS   Sphingopyxis bauzanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ99836.1, ECO:0000313|Proteomes:UP000197361};
RN   [1] {ECO:0000313|EMBL:OWQ99836.1, ECO:0000313|Proteomes:UP000197361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ99836.1,
RC   ECO:0000313|Proteomes:UP000197361};
RX   PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA   Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT   "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT   soil.";
RL   Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ99836.1}.
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DR   EMBL; NISK01000001; OWQ99836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246K2Y6; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000197361; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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:UP000197361};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..434
FT                   /note="peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012625457"
FT   DOMAIN          176..333
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
FT   REGION          28..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  45552 MW;  5E81DC98B90CFAE0 CRC64;
     MRRTRVFGFS FLVVLPLLAG CASVIPDSGS RPATTAPAPS QPTTAPRPYQ PRPSESGGVA
     AKPIPATPRA PFPAAAVPTD ATTAAASGIL AGPDFATLGV TADQAATALA AFRISCPSVQ
     RRADVSGLTQ GADWAESCNA AKNWSDSAAA AFFTRYFGTV QIGAGTAFVT GYYEPEIAGS
     RDRRPGYDIP IYRRPADLVD VDLGLFSDEL KDKKIRGRVE GSNLVQYYDR AAIESGALDG
     RGLEIAYAAD AAEFFFLQVQ GSGRLRLPDG GIMRIGYDTQ NGRGYVGIGK LLLDRGELQR
     GQASMQGILD YLRADPVRGA AVMNENPSWV FFREITGPGP LGAMGLPVTG RASVAADPKY
     VPLGAPVFLS LDRAEPNGLW IAQDTGGAIK GANRFDSFWG AGEDARAIAG GMAARGSALL
     LLPRASIARL IPAR
//