ID U2J258_9STRE Unreviewed; 429 AA.
AC U2J258;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=HMPREF1557_01859 {ECO:0000313|EMBL:ERJ74117.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ74117.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ74117.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ74117.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-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};
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:ERJ74117.1}.
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DR EMBL; AWVA01000110; ERJ74117.1; -; Genomic_DNA.
DR RefSeq; WP_019768975.1; NZ_KI259719.1.
DR AlphaFoldDB; U2J258; -.
DR PATRIC; fig|1227275.3.peg.1670; -.
DR HOGENOM; CLU_037608_1_0_9; -.
DR OrthoDB; 9812065at2; -.
DR Proteomes; UP000016617; 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; 3.90.640.30; -; 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 5..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..420
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 429 AA; 48242 MW; EAE0889FAAEE8D63 CRC64;
MRKQFYLLCA AVACAIILLG ILIVQYEIVK RDLARVTKRE LAYSKEQGAV TLVQKGSTFI
YYPSSEKGKV HDGVKEELAK LAKNSKDGDY RFIGLQYSDS NFNGVKEAKV YQHTYYKSLS
SLREGKRKVL ATFYVTTDHQ RLDLPDFLSR TTDLKADLAT RISQDQTLSQ NQQEKVLTSL
KETKLANLAF NLESSQLTFK LAGETINLPL TGLYNILNPN YLKGDDLETY KAYKRGDGRL
EKMSGHVVAL TFDDGPNPDT TPQVLKILKK YKAKATFFVV GKSVAGNEKI LKDELDDGHD
IGNHSWDHPQ LSKLPTTQAA SQINQTNQAI EQATGKAPIL LRPPYGATNP TVRSLTDLYQ
VLWDVDTYDW KYRNTQSILN QVKAQTQDGS VILMHDIHQT TVDALPTVLD YLSSQGYKFV
TVSQLYGYV
//
