ID C9A8P2_ENTCA Unreviewed; 506 AA.
AC C9A8P2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=ECBG_01122 {ECO:0000313|EMBL:EEV38853.1};
OS Enterococcus casseliflavus EC20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV38853.1, ECO:0000313|Proteomes:UP000012675};
RN [1] {ECO:0000313|EMBL:EEV38853.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV38853.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genome Sequencing Platform;
RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEV38853.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV38853.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC glucosamine + acetate.; EC=3.5.1.104;
CC Evidence={ECO:0000256|ARBA:ARBA00043715};
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DR EMBL; CP004856; EEV38853.1; -; Genomic_DNA.
DR RefSeq; WP_015510638.1; NZ_AKCC01000001.1.
DR AlphaFoldDB; C9A8P2; -.
DR GeneID; 15143769; -.
DR KEGG; ecas:ECBG_01122; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_037608_0_0_9; -.
DR Proteomes; UP000012675; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10954; CE4_CtAXE_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR017219; Peptidoglycan_deacetylase.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PIRSF; PIRSF037479; PG_GlcNAc_deacetylase; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037479-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000012675};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PIRSR:PIRSR037479-3}.
FT TRANSMEM 44..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..480
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-1"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-1"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-2"
FT SITE 429
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR037479-4"
SQ SEQUENCE 506 AA; 56678 MW; 21A1969D3B59C475 CRC64;
MPERKTYARR SDLHKKPSNN QKRTASAEER PKGLPSRKKP YRKAIFSLFA LLLIVLIATA
GSVLYTLHQQ EVAAQEKYEA AAEKLLASIQ AEQSQNGLKT TPEVLSKGAT KELIYRPQDL
DTFPIKDIKE RLTQAADHLR KKQTNKEVVT VARIQAQAAA SKVSTYSLKA DSYVWNRETG
RFEDAESLTD APIFVSEKTQ TELSLKELVP DEGSLLGIQQ VIQQKLLDQA KEPAKIIDAV
LAMERITFDS KFTYDPEKLT IELPKNQTGA TEITLPYSEI APFIDPDLVA ADQLNNALPS
LDPNKKYVAL TFDDGPNSTS TMDLLNILQE NDVKATFFML GQMVEQYPQA AKKVQEAGHE
IASHSYSHPQ LNTLSAEDLQ AEVTKTNKAI YNATGLLPRN LRPPYGAIDK QSAQTIGMPI
IQWDIDSQDW KLKDPKKINA LVQQNVFNGA MILIHDIHPK SVKAVPGVIK MLKNEGYEFV
TVDQLLEARQ KPLHQYFGMN DERLVD
//
