ID A0A0T7ZU50_STREE Unreviewed; 480 AA. AC A0A0T7ZU50; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 24-JAN-2024, entry version 35. DE SubName: Full=Peptidoglycan N-acetylglucosamine deacetylase A {ECO:0000313|EMBL:VMC88943.1}; GN Name=pgdA {ECO:0000313|EMBL:VMC88943.1}; GN ORFNames=ERS019171_01452 {ECO:0000313|EMBL:CIN74860.1}, GN SAMEA2627268_00726 {ECO:0000313|EMBL:VMC88943.1}; OS Streptococcus pneumoniae. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313 {ECO:0000313|EMBL:VMC88943.1, ECO:0000313|Proteomes:UP000311381}; RN [1] {ECO:0000313|EMBL:CIN74860.1, ECO:0000313|Proteomes:UP000041263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6B {ECO:0000313|Proteomes:UP000041263}, and SMRU13 RC {ECO:0000313|EMBL:CIN74860.1}; RG Pathogen Informatics; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:VMC88943.1, ECO:0000313|Proteomes:UP000311381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPSC47 {ECO:0000313|EMBL:VMC88943.1, RC ECO:0000313|Proteomes:UP000311381}; RG Pathogen Informatics; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CJZK01000018; CIN74860.1; -; Genomic_DNA. DR EMBL; CAAQRO010000003; VMC88943.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0T7ZU50; -. DR Proteomes; UP000041263; Unassembled WGS sequence. DR Proteomes; UP000311381; Unassembled WGS sequence. 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; cd10947; CE4_SpPgdA_BsYjeA_like; 1. DR Gene3D; 3.30.565.50; -; 1. DR Gene3D; 3.90.640.30; -; 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 InterPro; IPR040802; PgdA_N. DR PANTHER; PTHR10587:SF105; 4-DEOXY-4-FORMAMIDO-L-ARABINOSE-PHOSPHOUNDECAPRENOL DEFORMYLASE ARND-RELATED; 1. DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1. DR Pfam; PF18627; PgdA_N; 1. DR Pfam; PF01522; Polysacc_deac_1; 1. DR PIRSF; PIRSF037479; PG_GlcNAc_deacetylase; 1. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1. DR SUPFAM; SSF144015; Peptidoglycan deacetylase N-terminal noncatalytic region; 1. DR PROSITE; PS51677; NODB; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037479-3}; 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 34..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 285..459 FT /note="NodB homology" FT /evidence="ECO:0000259|PROSITE:PS51677" FT ACT_SITE 292 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-1" FT ACT_SITE 434 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-1" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3" FT BINDING 343 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3" FT BINDING 347 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-3" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-2" FT SITE 408 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000256|PIRSR:PIRSR037479-4" SQ SEQUENCE 480 AA; 54612 MW; A56912FCE3416B94 CRC64; MPNCIIEIIA QICYDINMNK SRLGRGRHGK TRHVLLALIG ILAISICLLG GFIAFKIYQQ KSFEQKIESL KKEKDDQLSE GNQKEHFRQG QAEVIAYYPL QGEKVISSVR ELINQDVKDK LESKDNLVFY YTEKEESGLK GVVNRNVTKQ IYDLVAFKIE ETEKTSLGKV HLTEDGQPFT LDQLFSDASK AKEQLIKELT SFIEDKKIEQ DQSEQIVKSF SDQDLSAWNF DYKDSQIILY PSSVVENLEE IALPVSAFFD VIQSSYLLEK DAALYQSYFD KKYQKVVALT FDDGPNPATT PQVLETLAKY DIKATFFVLG KNVSGNEDLV KRIKSEGHVV GNHSWSHPIL SQLSLDEAKK QITDTEDVLT KVLGSSSKLM RPPYGAITDD IRNSLDLSFI MWDVDSLDWK SKNEASILTE IQHQVANGSI VLMHDIHSPT VNALPRVIEY LKNQGYTFVT IPEMLNTRLK AHELYYSRDE //