ID E5WPE4_9BACI Unreviewed; 476 AA.
AC E5WPE4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=HMPREF1013_04331 {ECO:0000313|EMBL:EFV75553.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV75553.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV75553.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV75553.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV75553.1}.
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DR EMBL; ACWD01000061; EFV75553.1; -; Genomic_DNA.
DR RefSeq; WP_009335176.1; NZ_GL635755.1.
DR AlphaFoldDB; E5WPE4; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_037608_3_0_9; -.
DR Proteomes; UP000003283; 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; 3.30.565.40; Fervidobacterium nodosum Rt17-B1 like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 3.90.640.20; Heat-shock cognate protein, ATPase; 1.
DR InterPro; IPR021729; DUF3298.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR037126; PdaC/RsiV-like_sf.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF11738; DUF3298; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003283};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..454
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 476 AA; 53237 MW; 1B1EB5EEEA37E072 CRC64;
MLKRLKWPSW ALFCIFIAGI YYFISSGADT SLQAFSRTET TSPAAFPGLN LETRTKETKS
YTLAISTPIT EIENLNKPMK EWIQAQEMEF LELVKANRQV LDSEEFRAHL NIKAEPKKVS
DTMYTLVFEA YQYTGGANGQ AAVKTFTIDL ANQKMVHLAD VIRMDEESLA TLRPLIKKQI
GEKEELQDYL FEDLLDEALE NPSSWKWALS GKNFTLYFNE YEIAAGAAGA VKVKIPIEEI
RPLLKDEITQ HLKLPDIQLP EPEVKEPEAA PLDPNGKYIA LTFDDGPHPK VTPLILDILK
KHNAKATFYM LGSQAQFYPA LASQVAEEGH EIGNHSDSHA DLSSLGEIEI RKEMEEASTK
IKEASGQLPA TVRPPYGAMN EDVKKIAGMA HTPLILWSVD SLDWKTLNAA AIQKIVKANA
VPGAIVLMHD IHKPTAEALP DLLTYLEKEG YEFITVSQLL SLQEQEVTGT FFGKRQ
//
