DIGH_ECOL6
ID DIGH_ECOL6 Reviewed; 439 AA.
AC Q8CW29;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glycosyl hydrolase DigH {ECO:0000250|UniProtKB:P64426};
DE EC=3.2.1.- {ECO:0000250|UniProtKB:P64426};
DE AltName: Full=Divisome-localized glycosyl hydrolase {ECO:0000250|UniProtKB:P64426};
DE Flags: Precursor;
GN Name=digH {ECO:0000250|UniProtKB:P64426}; Synonyms=yddW;
GN OrderedLocusNames=c1920;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Divisome-localized glycosyl hydrolase that cleaves peptide-
CC free (denuded) peptidoglycans. {ECO:0000250|UniProtKB:P64426}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P64426}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Note=Localizes to the divisome.
CC {ECO:0000250|UniProtKB:P64426}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase-like 10 (GHL10) family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN80378.1; -; Genomic_DNA.
DR RefSeq; WP_000350354.1; NC_004431.1.
DR AlphaFoldDB; Q8CW29; -.
DR SMR; Q8CW29; -.
DR STRING; 199310.c1920; -.
DR EnsemblBacteria; AAN80378; AAN80378; c1920.
DR KEGG; ecc:c1920; -.
DR eggNOG; COG1649; Bacteria.
DR HOGENOM; CLU_019247_0_1_6; -.
DR OMA; YGPWSEY; -.
DR BioCyc; ECOL199310:C1920-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cell outer membrane; Cell wall biogenesis/degradation; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 28..439
FT /note="Glycosyl hydrolase DigH"
FT /id="PRO_0000013769"
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"
SQ SEQUENCE 439 AA; 49631 MW; EC7DABCEE6CEF6BE CRC64;
MDICSRNEKL AIRRPAILVA 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 TIKSIKPEVE FGVSPAGVWR
NRSHDPLGSD TRGAAAYDES YADTRRWVEQ GLLDYIAPQI YWPFSRSAAR YDVLAKWWAD
VVKPTRTRLY IGIAFYKVGE PSKIEPDWMI NGGVPELKKQ LDLNDALPEI SGTILFREDY
LNKPQTQQAV SYLQSRWGS
