DIGH_ECOLI
ID DIGH_ECOLI Reviewed; 439 AA.
AC P64426; P76130; Q2MBA2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycosyl hydrolase DigH {ECO:0000305};
DE EC=3.2.1.- {ECO:0000269|PubMed:32152098};
DE AltName: Full=Divisome-localized glycosyl hydrolase {ECO:0000303|PubMed:32152098};
DE Flags: Precursor;
GN Name=digH {ECO:0000303|PubMed:32152098}; Synonyms=yddW;
GN OrderedLocusNames=b1491, JW1486;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, OVEREXPRESSION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-236.
RX PubMed=32152098; DOI=10.1073/pnas.1919267117;
RA Yakhnina A.A., Bernhardt T.G.;
RT "The Tol-Pal system is required for peptidoglycan-cleaving enzymes to
RT complete bacterial cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:6777-6783(2020).
CC -!- FUNCTION: Divisome-localized glycosyl hydrolase that cleaves peptide-
CC free (denuded) peptidoglycans. Has either glucosaminidase or muramidase
CC activity. {ECO:0000269|PubMed:32152098}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:32152098}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Note=Localizes to the divisome.
CC {ECO:0000269|PubMed:32152098}.
CC -!- MISCELLANEOUS: Overexpression suppresses the chaining phenotype of the
CC tol-pal mutant. {ECO:0000269|PubMed:32152098}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase-like 10 (GHL10) family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74564.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76454.1; -; Genomic_DNA.
DR PIR; F64902; F64902.
DR RefSeq; NP_416008.1; NC_000913.3.
DR RefSeq; WP_000350395.1; NZ_STEB01000054.1.
DR AlphaFoldDB; P64426; -.
DR SMR; P64426; -.
DR BioGRID; 4263004; 204.
DR DIP; DIP-48187N; -.
DR IntAct; P64426; 2.
DR STRING; 511145.b1491; -.
DR PaxDb; P64426; -.
DR PRIDE; P64426; -.
DR EnsemblBacteria; AAC74564; AAC74564; b1491.
DR EnsemblBacteria; BAE76454; BAE76454; BAE76454.
DR GeneID; 58391399; -.
DR GeneID; 945975; -.
DR KEGG; ecj:JW1486; -.
DR KEGG; eco:b1491; -.
DR PATRIC; fig|1411691.4.peg.776; -.
DR EchoBASE; EB3555; -.
DR eggNOG; COG1649; Bacteria.
DR HOGENOM; CLU_019247_0_1_6; -.
DR InParanoid; P64426; -.
DR OMA; YGPWSEY; -.
DR PhylomeDB; P64426; -.
DR BioCyc; EcoCyc:G6785-MON; -.
DR PRO; PR:P64426; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0036405; C:anchored component of cell outer membrane; ISM:EcoCyc.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003790; GHL10.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF02638; GHL10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Cell wall biogenesis/degradation; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 28..439
FT /note="Glycosyl hydrolase DigH"
FT /id="PRO_0000013767"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 28
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 28
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 236
FT /note="D->N: Fails to enhance peptidoglycan cleavage in
FT combination with AmiD."
FT /evidence="ECO:0000269|PubMed:32152098"
SQ SEQUENCE 439 AA; 49574 MW; 3E74454C52F4F0F6 CRC64;
MDICSRNKKL TIRRPAILVA LALLLCSCKS TPPESMVTPP AGSKPPATTQ QSSQPMRGIW
LATVSRLDWP PVSSVNISNP TSRARVQQQA MIDKLDHLQR LGINTVFFQV KPDGTALWPS
KILPWSDLMT GKIGENPGYD PLQFMLDEAH KRGMKVHAWF NPYRVSVNTK PGTIRELNST
LSQQPASVYV QHRDWIRTSG DRFVLDPGIP EVQDWITSIV AEVVSRYPVD GVQFDDYFYT
ESPGSRLNDN ETYRKYGGAF ASKADWRRNN TQQLIAKVSH TIKSIKPGVE FGVSPAGVWR
NRSHDPLGSD TRGAAAYDES YADTRRWVEQ GLLDYIAPQI YWPFSRSAAR YDVLAKWWAD
VVKPTRTRLY IGIAFYKVGE PSKIEPDWMI NGGVPELKKQ LDLNDAVPEI SGTILFREDY
LNKPQTQQAV SYLQSRWGS
