HEXA_PORGI
ID HEXA_PORGI Reviewed; 777 AA.
AC P49008;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Beta-hexosaminidase;
DE EC=3.2.1.52;
DE AltName: Full=Beta-GlcNAcase;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE Short=Beta-NAHase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE Flags: Precursor;
GN Name=nahA; OrderedLocusNames=PG_0043;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=7881557; DOI=10.1099/13500872-140-12-3399;
RA Lovatt A., Roberts I.S.;
RT "Cloning and expression in Escherichia coli of the nahA gene from
RT Porphyromonas gingivalis indicates that beta-N-acetylhexosaminidase is an
RT outer-membrane-associated lipoprotein.";
RL Microbiology 140:3399-3406(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; X78979; CAA55582.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65295.1; -; Genomic_DNA.
DR RefSeq; WP_005873538.1; NC_002950.2.
DR AlphaFoldDB; P49008; -.
DR SMR; P49008; -.
DR STRING; 242619.PG_0043; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR EnsemblBacteria; AAQ65295; AAQ65295; PG_0043.
DR KEGG; pgi:PG_0043; -.
DR PATRIC; fig|242619.8.peg.39; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_5_0_10; -.
DR OMA; RIIWGVE; -.
DR OrthoDB; 727559at2; -.
DR BioCyc; PGIN242619:G1G02-39-MON; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
DR PROSITE; PS51820; PA14; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..777
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000012016"
FT DOMAIN 625..766
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="R -> H (in Ref. 1; CAA55582)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="E -> M (in Ref. 1; CAA55582)"
FT /evidence="ECO:0000305"
FT CONFLICT 282..283
FT /note="LA -> FR (in Ref. 1; CAA55582)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="T -> S (in Ref. 1; CAA55582)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="G -> A (in Ref. 1; CAA55582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 87661 MW; D0A55D2C2FFAD864 CRC64;
MKRLTFGACI CCLLSLMACS QKAKQVQIPE YDKGINIIPL PMQLTESDDS FEVDDKTTIC
VSAEELKPIA KLLADKLRAS ADLSLQIEIG EEPSGNAIYI GVDTALPLKE EGYMLRSDKR
GVSIIGKSAH GAFYGMQTLL QLLPAEVESS NEVLLPMTVP GVEIKDEPAF GYRGFMLDVC
RHFLSVEDIK KHIDIMAMFK INRFHWHLTE DQAWRIEIKK YPRLTEVGST RTEGDGTQYS
GFYTQEQVRD IVQYASDRFI TVIPEIEMPG HAMAALAAYP QLACFPREFK PRIIWGVEQD
VYCAGKDSVF RFISDVIDEV APLFPGTYFH IGGDECPKDR WKACSLCQKR MRDNGLKDEH
ELQSYFIKQA EKVLQKHGKR LIGWDEILEG GLAPSATVMS WRGEDGGIAA ANMNHDVIMT
PGSGGLYLDH YQGDPTVEPV AIGGYAPLEQ VYAYNPLPKE LPADKHRYVL GAQANLWAEY
LYTSERYDYQ AYPRLLAVAE LTWTPLAKKD FADFCRRLDN ACVRLDMHGI NYHIPLPEQP
GGSSDFIAFT DKAKLTFTTS RPMKMVYTLD ETEPTLTSTP YTVPLEFAQT GLLKIRTVTA
GGKMSPVRRI RVEKQPFNMS MEVPAPKPGL TIRTAYGDLY DVPDLQQVAS WEVGTVSSLE
EIMHGKEKIT SPEVLERRVV EATGYVLIPE DGVYEFSTEN NEFWIDNVKL IDNVGEVKKF
SRRNSSRALQ KGYHPIKTIW VGAIQGGWPT YWNYSRVMIR LKGEEKFKPI SSDMLFQ
