ID   MLTA_BUCAP              Reviewed;         366 AA.
AC   Q8K9A7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase A homolog;
DE            EC=4.2.2.n1;
DE   AltName: Full=Murein hydrolase A;
GN   Name=mltA; OrderedLocusNames=BUsg_442;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Note=In closely related bacteria this protein is
CC       attached to the outer membrane by a lipid anchor. This is apparently
CC       not the case here.
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DR   EMBL; AE013218; AAM67985.1; -; Genomic_DNA.
DR   RefSeq; WP_011053952.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9A7; -.
DR   SMR; Q8K9A7; -.
DR   STRING; 198804.BUsg_442; -.
DR   CAZy; GH102; Glycoside Hydrolase Family 102.
DR   EnsemblBacteria; AAM67985; AAM67985; BUsg_442.
DR   KEGG; bas:BUsg_442; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_2_0_6; -.
DR   OMA; DQNGHPY; -.
DR   OrthoDB; 1529555at2; -.
DR   Proteomes; UP000000416; Chromosome.
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; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR034654; MltA_3D.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; PTHR30124; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase.
FT   CHAIN           1..366
FT                   /note="Membrane-bound lytic murein transglycosylase A
FT                   homolog"
FT                   /id="PRO_0000196567"
SQ   SEQUENCE   366 AA;  42545 MW;  A07DCD520E5EAB72 CRC64;
     MLNSCINKIK KKKNIKKIIL MLIFIFSVNF FTKNTNQGKQ YEDKLNKDFT NIKKINIKNK
     LVNQKEFLLQ LEKIKIFSPN LYSKNISIYN AILKWLKKRA EINELNKFRI KLFQMKGVDQ
     YGNVKITGYY TPIVKASKIK KNNFIYPIYR TPSNFKKNEK LPQRKDIYNG FLKKEYILAY
     SDSLINNFIM EIQGSGFIDY GDNKPLIFFG YAKKNNWPYT SIGQILIKNG DIQKKNISMN
     TIKNWCTHHT QKEIQNLLEK NKSFVFFQET KRKEVYGSSA VPLVEKAAIA VDKSVIKIGS
     VVLVKIPVLD KNGIFIHKYE MHLLIALDVG GVIKGQHFDV YQGIGEKAGK LAGFYNHYGY
     AWVLKI