ID   F4QJQ4_9CAUL            Unreviewed;       406 AA.
AC   F4QJQ4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ABI_04370 {ECO:0000313|EMBL:EGF92005.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92005.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) 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};
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DR   EMBL; GL883077; EGF92005.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4QJQ4; -.
DR   STRING; 715226.ABI_04370; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_0_0_5; -.
DR   Proteomes; UP000006512; 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.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lipoprotein {ECO:0000313|EMBL:EGF92005.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          151..304
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   406 AA;  43883 MW;  DADA83E4A7D4DE87 CRC64;
     MTSLGDQPNV PAFLMTEGCM FRKIAIGFTL TAALLVSACV QTPSTPPVVT PPVVEPVPPV
     TPPVTPVANP VPANKRLDTL PGWVDSDAFI ALEALRATCI YKAGRQYAAV CADLKDEEFN
     TPADIKAFLI TRFQVEAVPG EGLLTGYYVP DYQAEYAPTT EFSQPVRPKP DDLVVIPGSQ
     LTPPSTAVKI AARKVGDKYV PYYTRAEIEL MPVATSYYMR PEDYFFMQLQ GSAFLTTPDG
     KTVYSAYAAD NGRPFVGIAK VMQERGYLAP NQTSGDNIHK WLAEHRGPEA TEVMNINPRY
     GFFVIQPDRT APVGASGLSL PPGSAIAVDP TLNPLGDLFW IDANAGTLAD AFPVYQRMVS
     ALDTGGAIKG QIRADLYVGH GAKAGTEAGR IKHKLKMWRI VPFVGN
//