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Database: UniProt
Entry: A0A0M5JQW7_9GAMM
LinkDB: A0A0M5JQW7_9GAMM
Original site: A0A0M5JQW7_9GAMM 
ID   A0A0M5JQW7_9GAMM        Unreviewed;      1082 AA.
AC   A0A0M5JQW7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:ALD03102.1};
GN   ORFNames=AMQ28_12575 {ECO:0000313|EMBL:ALD03102.1};
OS   Acinetobacter sp. TTH0-4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD03102.1, ECO:0000313|Proteomes:UP000055186};
RN   [1] {ECO:0000313|EMBL:ALD03102.1, ECO:0000313|Proteomes:UP000055186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD03102.1,
RC   ECO:0000313|Proteomes:UP000055186};
RA   Zhang G.;
RT   "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT   permafrost region.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; CP012608; ALD03102.1; -; Genomic_DNA.
DR   RefSeq; WP_053579897.1; NZ_CP012608.1.
DR   AlphaFoldDB; A0A0M5JQW7; -.
DR   STRING; 1646498.AMQ28_12575; -.
DR   KEGG; att:AMQ28_12575; -.
DR   PATRIC; fig|1646498.3.peg.2530; -.
DR   Proteomes; UP000055186; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd00118; LysM; 8.
DR   CDD; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 8.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   Pfam; PF01476; LysM; 8.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 8.
DR   SUPFAM; SSF54106; LysM domain; 8.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 8.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          584..628
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          647..691
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          718..763
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          796..840
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          848..892
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          916..960
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          986..1030
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          1035..1079
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          363..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..979
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1082 AA;  117218 MW;  BAC536F17B1DE3A6 CRC64;
     MYKPTAILLQ PSFPHFFKIT VLGSALAALG LTGCSSSQSA TQSSKSNMVG SGYLDANSLD
     SLEDLLSATD MRAVEGDRLL ILKHGDVWKR MTVGFKMDQT HWDSRIEAQR GWFISRQPYL
     DRLSARASRY LYHTVKEAER RGLPTELALL PIIESSYDPA ATSSAAAAGM WQFIPSTGRI
     YGLKQTSLYD GRRDVVESTR AAYEFLGSLY NQFGSWELAL AAYNAGPGRI QQAINRNKAA
     GLPTDYWSLK LPQETMNYVP RFLAVAQIIK NPNAYGVSLP PIANRPHFRE IAVGPVNLNE
     IASITGLSRA ELYQLNPGHR GDQIDSQSPM RIIIPADLSP SIDARIKKLS PNSGGLWANT
     AKPFTPEKSN PPTLNTQQIT PAKTAPPALK SNTTVVTTAS KTPTASNPVL AAASKSKSTP
     QGSAALASFA ANSDIPSAPR IPVAVNQVAN VKPISVEPAL SAAEREQILA AVKAEGENKT
     VEQVLQPVAS KAEQEKVVEE LKALAPQGTE IVDPFDGKIK LTAIQTSQSI AEQQGKELTR
     GFAYPKGVAE NTRADSEEAK RNQGKNYVRT DSEVVVSPPK GKRSTYTVLP GDTLAVIAMK
     NGLNWRDVAK WNQIDPKSPL FVGTSIYLYD AKPQNTEAST PVKSKAESYV VQANDNLTGV
     ANQFGLSVKQ LADYNNLSLN SGLRVGQKLN LRETVQTSPS ISDTQVARSN AVSKIKTKPY
     VVKRGEYLKL IAERYALSNQ ELADLTTGLT SSSSLLMGQK INVPLQTIES KSDNQSNEKI
     SSKIDNVSVE PTYKVENYQV QRGDTLTSIA LQSKISLTEL AELNKISNTG GLRLGQVIKI
     PAGSTVPETY TVQSGDSLSV ISAKYNVGMD YIANLNGISR TTGLRVGQRL KLTGKETAST
     RTDANVEKSN TQKNSDIHLV KSGETLSSIA KKYHLQLNYL AELNDLSRTA NVRVGQRLKV
     EGEADQAETK SEVKTAKTSK NSKNTDSYTV KSGESLNVIA NRVGISVAEL AELNDLNARS
     GLRVGQQITI PKVVTEYKIQ RGDTLIGLAN RYGLDTAKLA EMNAMQPNTQ LRIGAIIKVP
     NL
//
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