ID K1LXX5_9LACT Unreviewed; 444 AA.
AC K1LXX5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN ORFNames=HMPREF9706_01058 {ECO:0000313|EMBL:EKB54868.1};
OS Facklamia hominis CCUG 36813.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB54868.1, ECO:0000313|Proteomes:UP000004465};
RN [1] {ECO:0000313|EMBL:EKB54868.1, ECO:0000313|Proteomes:UP000004465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB54868.1,
RC ECO:0000313|Proteomes:UP000004465};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL Submitted (JUL-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:EKB54868.1}.
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DR EMBL; AGZD01000007; EKB54868.1; -; Genomic_DNA.
DR RefSeq; WP_006908379.1; NZ_JH932292.1.
DR AlphaFoldDB; K1LXX5; -.
DR STRING; 883111.HMPREF9706_01058; -.
DR PATRIC; fig|883111.3.peg.1063; -.
DR HOGENOM; CLU_050027_0_0_9; -.
DR OrthoDB; 9812065at2; -.
DR Proteomes; UP000004465; 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 CDD; cd10917; CE4_NodB_like_6s_7s; 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 PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 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:UP000004465};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..430
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 444 AA; 50483 MW; B03C058CFAD173BB CRC64;
MRKIKKINFQ PKIFSPKVGA VLLGLVVCLL IVYWQKPSKA LVNQYQVALD QLQSETKGLD
KNAKQEDLDH LAAIVNQMPL VGGLPFKKKY VTFQRAFDEL QNARSIFQTN QGDNKLLRAD
LDRKELEGKL KACQGKEANS PACQIYQEGM DILQSIDEAQ AVVQNRDLNI KVRGDIEPGL
KEYLKFEARY RDLANQPQAE SLRQTLQSKA DRLAEIILKG AQYGDYSAEF KENLKESPFL
KIALRASEFD QEPLASLTFD DGPNPEYTPW LLDVLKKHGV KATFFLVGGN VDKYPELTKR
IYDEGHIIGN HTYNHPDLRK CSDEEVLKQF EWTQMAIKAA CGFEPNLYRL PFGAGGKRVV
DLMAKQGMTS ILWNIDTMDW SSHNTQAILN EVDRSLQHHS LILMHDNHPA TPEAVDQLIP
KLKELGYAFV GPDELSFKLR YFSE
//
