ID D3NW10_AZOS1 Unreviewed; 397 AA.
AC D3NW10;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
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 Name=mltA {ECO:0000313|EMBL:BAI72589.1};
GN OrderedLocusNames=AZL_019510 {ECO:0000313|EMBL:BAI72589.1};
OS Azospirillum sp. (strain B510).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI72589.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI72589.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI72589.1,
RC ECO:0000313|Proteomes:UP000002040};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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; AP010946; BAI72589.1; -; Genomic_DNA.
DR AlphaFoldDB; D3NW10; -.
DR STRING; 137722.AZL_019510; -.
DR CAZy; GH102; Glycoside Hydrolase Family 102.
DR KEGG; azl:AZL_019510; -.
DR HOGENOM; CLU_037751_0_0_5; -.
DR Proteomes; UP000002040; 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; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT DOMAIN 159..291
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 397 AA; 42912 MW; 478ECD6B2FAAF670 CRC64;
MLVAECAMAA AAGKTCARDG AWVKGLRLSM MGGLLATLAA CAGTAPTVDG QRRTAQRPTW
DQVAPDFRRL AGWIDDDHAQ AVPAVQRTCG WVGNQPPGKP LGPLRTAGTT DDWRAICAAA
RDLPPGDSEA ARRFFETFFT PRDVGNGETG LFTGYYEIEL HGSWTPSARY TVPLYRMPQR
GKNGLPSRAR IEAGALKGKG LELMWVDDPI DAFFLEIQGS GRAIMADGSV VGIHYSGQNG
HSYYPIGRHI IDIGDATPEQ MSLQTIRRWL KDHPAEAQRV MNLNPSYVFF KVKPEVGARG
ARNMELTPGR SLAVDAEHIP LGVPLWLEVR DAPVPGGAIN RLVVAQDTGG AIKGPVRGDL
FWGHGPQAEE GAGVMKARGH YTMLAPRTLS VETAQRK
//
