ID   MLTA_BUCAI              Reviewed;         359 AA.
AC   P57531;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=BU458;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13155.1; -; Genomic_DNA.
DR   RefSeq; NP_240269.1; NC_002528.1.
DR   RefSeq; WP_009874410.1; NC_002528.1.
DR   AlphaFoldDB; P57531; -.
DR   SMR; P57531; -.
DR   STRING; 107806.10039121; -.
DR   CAZy; GH102; Glycoside Hydrolase Family 102.
DR   EnsemblBacteria; BAB13155; BAB13155; BAB13155.
DR   KEGG; buc:BU458; -.
DR   PATRIC; fig|107806.10.peg.467; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_2_0_6; -.
DR   OMA; DQNGHPY; -.
DR   Proteomes; UP000001806; 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   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Membrane-bound lytic murein transglycosylase A
FT                   homolog"
FT                   /id="PRO_0000196566"
SQ   SEQUENCE   359 AA;  41773 MW;  24E12A2778D351AB CRC64;
     MQKKIIKTII FFSLFFLFEK SYAYININQG QQYEKKLIQN LTKIKQINIK KKIINAESFY
     IQVEKIKKFS PSLYLKNEST YKTILKWLKK NSNINELNEF GINLFQMKGI DNYGNVKITG
     YYTPIVQARK IKKNNFKYPI YSMPYHLKKN EPLPKRKDIY NGVLDKKYIL AYSNSLIDNF
     IMEIQGSAFI DYGNKKKLIF FSYAGKNGWP YKSIGQILIN RGDIEKKNMS MQAINKWFTK
     HTNKEIQDLF EKNESFVFFK ETKKKQVYGA SAVPLIAQTS VAADNSIIKK GSVILLKIPI
     LDQNGVFLNK YEMRLVIALD VGGAIKGHHF DIYEGIGTKA SILSGYYNHY GYAWILNKK