ID I0SHX2_STRAP Unreviewed; 454 AA.
AC I0SHX2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=HMPREF1043_1215 {ECO:0000313|EMBL:EID22975.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID22975.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID22975.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID22975.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID22975.1}.
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DR EMBL; AICP01000030; EID22975.1; -; Genomic_DNA.
DR RefSeq; WP_003034939.1; NZ_AICP01000030.1.
DR AlphaFoldDB; I0SHX2; -.
DR PATRIC; fig|1095729.3.peg.696; -.
DR Proteomes; UP000003245; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR040802; PgdA_N.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF18627; PgdA_N; 1.
DR Pfam; PF01522; Polysacc_deac_1; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..434
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 454 AA; 52124 MW; BA29B308EA6D381F CRC64;
MKKILLIVLN VAFLMIIIFG SFRIRKLLQE RKLNRQISQV LKRADTKYHY GSVRKQTGRV
GSQLITSYYP LTESKQDIGV IKEKINADIQ KFSDKQSQVS QYDNLIFYVS HFTETNFSGV
KQVEIKRISY PVLTTKVGKA REEVLDSLYM SSDNKLFSLN RLFKNTEQAK KLLLEEMQQQ
ITALHKTEGQ KILQAFQTRD ISQWTFSYEK GKLNLFYKNN DRVSKVEIAL PALYEVIDDH
YLKEEDLAAY QSYQAKKQQK LVALTFDDGP NAATTPQALD ILAKYHVKGT FFMLGKNIAG
NEQLVKRVHD EGHEIGNHSW SHPQLPTLAL EQAKKQIEDT QAALRAVIGE SPKMMRPPYG
AINNTLRNAV DMSFIMWNVD SLDWKNRNTG SIMEQVKKQT CPGSIILMHD IHQTTINALP
SVIEYLQKNG YTLVTVSELL NHRLEGHRLY YGAN
//
