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DIGH_ECO57
ID   DIGH_ECO57              Reviewed;         439 AA.
AC   P64427; P76130;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=Z2217, ECs2096;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56277.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35519.1; -; Genomic_DNA.
DR   PIR; H90890; H90890.
DR   RefSeq; NP_310123.1; NC_002695.1.
DR   RefSeq; WP_000350395.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P64427; -.
DR   SMR; P64427; -.
DR   STRING; 155864.EDL933_2149; -.
DR   EnsemblBacteria; AAG56277; AAG56277; Z2217.
DR   EnsemblBacteria; BAB35519; BAB35519; ECs_2096.
DR   GeneID; 58391399; -.
DR   GeneID; 917296; -.
DR   KEGG; ece:Z2217; -.
DR   KEGG; ecs:ECs_2096; -.
DR   PATRIC; fig|386585.9.peg.2201; -.
DR   eggNOG; COG1649; Bacteria.
DR   HOGENOM; CLU_019247_0_1_6; -.
DR   OMA; YGPWSEY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; 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_0000013768"
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;  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
 
 
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