ID A0A1T4N849_VIBCI Unreviewed; 367 AA.
AC A0A1T4N849;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Membrane-bound lytic murein transglycosylase A {ECO:0000256|PIRNR:PIRNR019422};
DE EC=4.2.2.n1 {ECO:0000256|PIRNR:PIRNR019422};
DE AltName: Full=Murein hydrolase A {ECO:0000256|PIRNR:PIRNR019422};
GN ORFNames=SAMN02745782_01246 {ECO:0000313|EMBL:SJZ75008.1};
OS Vibrio cincinnatiensis DSM 19608.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1123491 {ECO:0000313|EMBL:SJZ75008.1, ECO:0000313|Proteomes:UP000190834};
RN [1] {ECO:0000313|EMBL:SJZ75008.1, ECO:0000313|Proteomes:UP000190834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19608 {ECO:0000313|EMBL:SJZ75008.1,
RC ECO:0000313|Proteomes:UP000190834};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC muropeptides during cell elongation and/or cell division.
CC {ECO:0000256|PIRNR:PIRNR019422}.
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 ECO:0000256|PIRNR:PIRNR019422};
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DR EMBL; FUXB01000005; SJZ75008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4N849; -.
DR STRING; 1123491.SAMN02745782_01246; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000190834; 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-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
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; 2.
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 ECO:0000256|PIRNR:PIRNR019422};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422}.
FT DOMAIN 119..252
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 367 AA; 40374 MW; 279C00B8CEDD028B CRC64;
MIKRFFSYAT LAFLFGCAQP TDRAQQYLDD EFPQILNKVD SVASNSPRDF SAFAAQSEQV
VTRSASMAAI YQSLYEKLNE WVLQSGDPAE LAQFGIQTAQ LGGGDKQGNV LFTGYFSPVM
ELRHTPDEVF RYPVYALPEC DVDCPTRAEI YAGALDGQGL ELGYSANLID PFIMEVQGSG
FVHFEDDDTL EYFAYAGKNN RAYVSIGRIL IERGFVKRAD MSLKAIKEWV LANDEATVKE
LLEQNPSYVF FRPSAAAPVT GSAGIPLLPM ASVAGDRTLF PMGTPILAEV PLLNADGTWS
GAHQLRLLIV LDTGGAVKQN HLDLYHGMGP RAGIEAGHYK HFGRVWKLGL DNSPTQAPWA
LSPEKRE
//
