ID A0A1H7GGM6_STIAU Unreviewed; 397 AA.
AC A0A1H7GGM6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05444354_101352 {ECO:0000313|EMBL:SEK34925.1};
OS Stigmatella aurantiaca.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=41 {ECO:0000313|EMBL:SEK34925.1, ECO:0000313|Proteomes:UP000182719};
RN [1] {ECO:0000313|Proteomes:UP000182719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17044 {ECO:0000313|Proteomes:UP000182719};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOAP01000001; SEK34925.1; -; Genomic_DNA.
DR RefSeq; WP_075004624.1; NZ_FOAP01000001.1.
DR AlphaFoldDB; A0A1H7GGM6; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000182719; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000182719};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..397
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010300185"
FT DOMAIN 134..291
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 397 AA; 43309 MW; C4B37BEAF3998559 CRC64;
MRLSHALGWA ACLLLATACS RAARAPITRP EEALVPLSRP LELSDDGDAE SLRTAISQSL
TWLRAQPAGK GFVFGPRTVT AGEMRDALER LSARVTPGLT PAELTRRVLE DFEWMEAAGG
EDGTVLFTGY YEPLIDASLS PTGEYATPIH GPPADLLEIS LEPFAERFKA ERLFGRLDGR
RVVPYWTRSE IRGGKLGNQK LELAWAKDPV ALFFLEVQGS GILRLPDGTE RRVGYAASNG
RPYRSIGALL IQEGAIPRET MSMQALRGWL ALNPAQCHRV LDHNESYVFF RFLEGAAVGS
LGRPVTPGRS IATDARLFPR GALAYIRTER PVARAGGQVA WQPLSRFVLN QDTGGAIRGA
GRVDVFWGRG ADAELAAGLM KQKGRLLFLV PRAPRTP
//