ID A0A2S2CWQ4_9PROT Unreviewed; 742 AA.
AC A0A2S2CWQ4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:AWK88942.1};
GN ORFNames=DEW08_23165 {ECO:0000313|EMBL:AWK88942.1};
OS Azospirillum thermophilum.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AWK88942.1,
OG ECO:0000313|Proteomes:UP000245629}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88942.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RC PLASMID=unnamed1 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: Belongs to the virb1 family.
CC {ECO:0000256|ARBA:ARBA00009387}.
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DR EMBL; CP029356; AWK88942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CWQ4; -.
DR KEGG; azz:DEW08_23165; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000245629; Plasmid unnamed1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd13401; Slt70-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:AWK88942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245629};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 503..608
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 154..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 79864 MW; 7F54D2233C2CEA28 CRC64;
MLRIFCSAAN SVGPTASLQR NLLGALGIAV VLAAAPDGLD GYRPARAALV IHAPDGRPVT
PPGHARADQP LLLATDEEAR AVQLGEEDAG RYRRIFLLQE RAEWDAADAE IRQLSDTRLL
GYVLRQRYLH PDRRASYEEL AGWMQRYADH AGAERVHGLA QRRQPAGQRP PKAPNSERGE
RLSGSLERLG GLRTVSEKRA AEKQGADRQA GEERTDEAAP SPIASGEESV TVAPRSRTVS
RPRTDRAAIA RIEDLLRSGK PGPALSLLNQ DEFGRSLDTA QYDLARSRIA AALYYAGDVG
EALSLASASA SRSGQLLPEA HWIAGLAAYR LKQVDRASRH FDAMAAGAPR SPWLAAAGHY
WAARMHKLKG RNGQAGEQLL AAARYSHTFY GLVALRALGD TGSLRWQAPE LSGRQLKALA
ERPEGLRAIA LLQADQRDLA EMELQRIHPK GNALIEQALV TLADRAGLPA LSLQIGNAVA
GPDGAPYAAA LYPLPHWKPR DGFALDRALV FAVMRQESRF DPRLVSSAGA TGLMQIMPAT
AQHVQERNAD IGDADTDRSA LFDPARNMEL GQRYLAELLT MPEIGGNLFL AAAAYNAGPG
TLMRWRRDLS DVTDPLLFIE SLPFAETRDY VEKVLANFWI YRLRLGQETA SLDAVAAGGW
PVYIAEDKRP AVEPTLVATK PPADLRPDAV PEAAPVPQEA PGIETATAAE AVPQGVLPGG
ALSGSSVAER ETATPDGSDA KD
//
