ID   A0A1T4XBX4_9GAMM        Unreviewed;       422 AA.
AC   A0A1T4XBX4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN02745130_02751 {ECO:0000313|EMBL:SKA86897.1};
OS   Thiothrix eikelboomii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA86897.1, ECO:0000313|Proteomes:UP000190460};
RN   [1] {ECO:0000313|EMBL:SKA86897.1, ECO:0000313|Proteomes:UP000190460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA86897.1,
RC   ECO:0000313|Proteomes:UP000190460};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUYB01000015; SKA86897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4XBX4; -.
DR   STRING; 92487.SAMN02745130_02751; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000190460; 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   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   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 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:UP000190460}.
FT   DOMAIN          184..313
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   422 AA;  47228 MW;  F6FFC096B730D437 CRC64;
     MKVNRVSRVL SLVSTALCVG GWYAEALQAD VLPWSNYHAP EIALPLYQPT DRAKAEAFFP
     LNIPSAQTAK FVPKHAAPLP TFFPEQQTCN PSHFSLDACI LKTVASQEGL LQQITYLRSR
     NPQRREGAHW ANLPNQVLLQ TAVELMRWGH GQAPYTLQEG FNLLEIPSAK HTSQAQYTGY
     FTPVVEVQTW PDAQYRYPIY SSPVGADSNF SRAEIDAGAL QGKGLEIGWT NDLVNLYFAH
     IQGSAIARFT DGQEVFLDYA GTNNKQHISI GEYLQNQGYQ GSLSNAKMRQ WLYQHPERMT
     EVLHQNPRYV FFKKTNTRPK TSIGSEVIPW HTVAVDDNFI PLGSVLLAEI PRVSRQGEIV
     GSDWRLLFAQ DRGQAIKGPG RLDFYTGFGP AAEQATYHVT GLRKSYLMVL KPEVFRKSGA
     GL
//