ID STRH_STRPN Reviewed; 1312 AA. AC P49610; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 27-MAR-2024, entry version 148. DE RecName: Full=Beta-N-acetylhexosaminidase; DE EC=3.2.1.52; DE Flags: Precursor; GN Name=strH; OrderedLocusNames=SP_0057; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 12213; RX PubMed=7721787; DOI=10.1074/jbc.270.15.8805; RA Clarke V.A., Platt N., Butters T.D.; RT "Cloning and expression of the beta-N-acetylglucosaminidase gene from RT Streptococcus pneumoniae. Generation of truncated enzymes with modified RT aglycon specificity."; RL J. Biol. Chem. 270:8805-8814(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., RA Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). 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: Secreted, cell wall {ECO:0000255|PROSITE- CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00477}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L36923; AAC41450.1; -; Genomic_DNA. DR EMBL; AE005672; AAK74246.1; -; Genomic_DNA. DR PIR; A56390; A56390. DR PIR; E95006; E95006. DR RefSeq; WP_000679952.1; NZ_CP089948.1. DR PDB; 2LTJ; NMR; -; A=1050-1140. DR PDB; 2YL5; X-ray; 2.15 A; A/B/C/D=627-1064. DR PDB; 2YL6; X-ray; 1.60 A; A=181-614. DR PDB; 2YL8; X-ray; 1.75 A; A=181-614. DR PDB; 2YL9; X-ray; 2.65 A; A/B/C/D=627-1062. DR PDB; 2YLA; X-ray; 2.70 A; A/B/C/D=627-1064. DR PDB; 2YLL; X-ray; 1.85 A; A=181-614. DR PDB; 4AZ5; X-ray; 1.73 A; A=181-614. DR PDB; 4AZ6; X-ray; 1.36 A; A=181-613. DR PDB; 4AZ7; X-ray; 1.70 A; A=181-613. DR PDB; 4AZB; X-ray; 2.10 A; A=181-614. DR PDB; 4AZC; X-ray; 2.09 A; A/B/C/D=627-1064. DR PDB; 4AZG; X-ray; 2.40 A; A/B=627-1064. DR PDB; 4AZH; X-ray; 2.22 A; A/B/C/D=627-1064. DR PDB; 4AZI; X-ray; 1.98 A; A/B=627-1064. DR PDBsum; 2LTJ; -. DR PDBsum; 2YL5; -. DR PDBsum; 2YL6; -. DR PDBsum; 2YL8; -. DR PDBsum; 2YL9; -. DR PDBsum; 2YLA; -. DR PDBsum; 2YLL; -. DR PDBsum; 4AZ5; -. DR PDBsum; 4AZ6; -. DR PDBsum; 4AZ7; -. DR PDBsum; 4AZB; -. DR PDBsum; 4AZC; -. DR PDBsum; 4AZG; -. DR PDBsum; 4AZH; -. DR PDBsum; 4AZI; -. DR AlphaFoldDB; P49610; -. DR SMR; P49610; -. DR CAZy; GH20; Glycoside Hydrolase Family 20. DR PaxDb; 170187-SP_0057; -. DR EnsemblBacteria; AAK74246; AAK74246; SP_0057. DR KEGG; spn:SP_0057; -. DR eggNOG; COG3064; Bacteria. DR eggNOG; COG3525; Bacteria. DR eggNOG; COG3583; Bacteria. DR BioCyc; SPNE170187:G1FZB-64-MONOMER; -. DR Proteomes; UP000000585; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. 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 CDD; cd06564; GH20_DspB_LnbB-like; 2. DR Gene3D; 1.20.1270.90; AF1782-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 2. DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 2. DR InterPro; IPR011098; G5_dom. DR InterPro; IPR015883; Glyco_hydro_20_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR019931; LPXTG_anchor. DR InterPro; IPR005877; YSIRK_signal_dom. DR NCBIfam; TIGR01167; LPXTG_anchor; 1. DR NCBIfam; TIGR01168; YSIRK_signal; 1. DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1. DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1. DR Pfam; PF07501; G5; 2. DR Pfam; PF00728; Glyco_hydro_20; 2. DR Pfam; PF00746; Gram_pos_anchor; 1. DR Pfam; PF04650; YSIRK_signal; 1. DR SMART; SM01208; G5; 2. DR SUPFAM; SSF51445; (Trans)glycosidases; 2. DR PROSITE; PS51109; G5; 2. DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell wall; Glycosidase; Hydrolase; Peptidoglycan-anchor; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..33 FT /evidence="ECO:0000255" FT CHAIN 34..1284 FT /note="Beta-N-acetylhexosaminidase" FT /id="PRO_0000012020" FT PROPEP 1285..1312 FT /note="Removed by sortase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT /id="PRO_0000012021" FT DOMAIN 1059..1138 FT /note="G5 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437" FT DOMAIN 1150..1230 FT /note="G5 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437" FT REGION 38..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 176..616 FT /note="Catalytic domain 1" FT REGION 621..1046 FT /note="Catalytic domain 2" FT REGION 1244..1290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1281..1285 FT /note="LPXTG sorting signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT COMPBIAS 38..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..104 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..120 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1284 FT /note="Pentaglycyl murein peptidoglycan amidated threonine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT CONFLICT 39 FT /note="Missing (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="V -> E (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="A -> E (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 617 FT /note="Q -> L (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 1045 FT /note="V -> A (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 1161 FT /note="E -> K (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 1171 FT /note="C -> R (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT CONFLICT 1267 FT /note="V -> A (in Ref. 1; AAC41450)" FT /evidence="ECO:0000305" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 186..193 FT /evidence="ECO:0007829|PDB:4AZ6" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 201..214 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 218..228 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 246..260 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 271..283 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 287..297 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 299..308 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 314..317 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 320..326 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 331..348 FT /evidence="ECO:0007829|PDB:4AZ6" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 353..358 FT /evidence="ECO:0007829|PDB:4AZ6" FT TURN 362..368 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 371..380 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:4AZB" FT HELIX 390..407 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 411..416 FT /evidence="ECO:0007829|PDB:4AZ6" FT TURN 417..420 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 421..423 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 435..438 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 451..456 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 484..493 FT /evidence="ECO:0007829|PDB:4AZ6" FT STRAND 510..517 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 527..540 FT /evidence="ECO:0007829|PDB:4AZ6" FT TURN 541..544 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 550..557 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 568..582 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 593..608 FT /evidence="ECO:0007829|PDB:4AZ6" FT HELIX 627..630 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 631..638 FT /evidence="ECO:0007829|PDB:4AZI" FT TURN 639..641 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 646..659 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 663..673 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 682..684 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 687..689 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 691..705 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 716..728 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 732..742 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 744..752 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 759..770 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 775..792 FT /evidence="ECO:0007829|PDB:4AZI" FT TURN 793..795 FT /evidence="ECO:0007829|PDB:4AZC" FT STRAND 796..802 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 808..810 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 815..821 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 825..841 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 845..850 FT /evidence="ECO:0007829|PDB:4AZI" FT TURN 851..854 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 855..857 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 868..871 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 884..889 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 893..896 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 899..901 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 902..904 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 909..911 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 916..925 FT /evidence="ECO:0007829|PDB:4AZI" FT TURN 936..938 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 943..951 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 961..974 FT /evidence="ECO:0007829|PDB:4AZI" FT TURN 975..978 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 984..990 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 1002..1013 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 1021..1023 FT /evidence="ECO:0007829|PDB:4AZI" FT HELIX 1024..1036 FT /evidence="ECO:0007829|PDB:4AZI" FT STRAND 1055..1058 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1060..1063 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1065..1073 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1085..1088 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1092..1094 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1099..1109 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1118..1120 FT /evidence="ECO:0007829|PDB:2LTJ" FT STRAND 1131..1134 FT /evidence="ECO:0007829|PDB:2LTJ" SQ SEQUENCE 1312 AA; 144550 MW; 503375B5257A90B5 CRC64; MKHEKQQRFS IRKYAVGAAS VLIGFAFQAQ TVAADGVTPT TTENQPTIHT VSDSPQSSEN RTEETPKAVL QPEAPKTVET ETPATDKVAS LPKTEEKPQE EVSSTPSDKA EVVTPTSAEK ETANKKAEEA SPKKEEAKEV DSKESNTDKT DKDKPAKKDE AKAEADKPAT EAGKERAATV NEKLAKKKIV SIDAGRKYFS PEQLKEIIDK AKHYGYTDLH LLVGNDGLRF MLDDMSITAN GKTYASDDVK RAIEKGTNDY YNDPNGNHLT ESQMTDLINY AKDKGIGLIP TVNSPGHMDA ILNAMKELGI QNPNFSYFGK KSARTVDLDN EQAVAFTKAL IDKYAAYFAK KTEIFNIGLD EYANDATDAK GWSVLQADKY YPNEGYPVKG YEKFIAYAND LARIVKSHGL KPMAFNDGIY YNSDTSFGSF DKDIIVSMWT GGWGGYDVAS SKLLAEKGHQ ILNTNDAWYY VLGRNADGQG WYNLDQGLNG IKNTPITSVP KTEGADIPII GGMVAAWADT PSARYSPSRL FKLMRHFANA NAEYFAADYE SAEQALNEVP KDLNRYTAES VTAVKEAEKA IRSLDSNLSR AQQDTIDQAI AKLQETVNNL TLTPEAQKEE EAKREVEKLA KNKVISIDAG RKYFTLNQLK RIVDKASELG YSDVHLLLGN DGLRFLLDDM TITANGKTYA SDDVKKAIIE GTKAYYDDPN GTALTQAEVT ELIEYAKSKD IGLIPAINSP GHMDAMLVAM EKLGIKNPQA HFDKVSKTTM DLKNEEAMNF VKALIGKYMD FFAGKTKIFN FGTDEYANDA TSAQGWYYLK WYQLYGKFAE YANTLAAMAK ERGLQPMAFN DGFYYEDKDD VQFDKDVLIS YWSKGWWGYN LASPQYLASK GYKFLNTNGD WYYILGQKPE DGGGFLKKAI ENTGKTPFNQ LASTKYPEVD LPTVGSMLSI WADRPSAEYK EEEIFELMTA FADHNKDYFR ANYNALREEL AKIPTNLEGY SKESLEALDA AKTALNYNLN RNKQAELDTL VANLKAALQG LKPAVTHSGS LDENEVAANV ETRPELITRT EEIPFEVIKK ENPNLPAGQE NIITAGVKGE RTHYISVLTE NGKTTETVLD SQVTKEVINQ VVEVGAPVTH KGDESGLAPT TEVKPRLDIQ EEEIPFTTVT CENPLLLKGK TQVITKGVNG HRSNFYSVST SADGKEVKTL VNSVVAQEAV TQIVEVGTMV THVGDENGQA AIAEEKPKLE IPSQPAPSTA PAEESKVLPQ DPAPVVTEKK LPETGTHDSA GLVVAGLMST LAAYGLTKRK ED //