GenomeNet

Database: UniProt
Entry: A0A1H7GGM6_STIAU
LinkDB: A0A1H7GGM6_STIAU
Original site: A0A1H7GGM6_STIAU 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system