ID A0A0U1KMM0_9BACI Unreviewed; 1031 AA.
AC A0A0U1KMM0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 02-APR-2025, entry version 39.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
DE Flags: Precursor;
GN Name=nanA_2 {ECO:0000313|EMBL:CQR47247.1};
GN ORFNames=BN1058_01554 {ECO:0000313|EMBL:CQR47247.1};
OS Paraliobacillus sp. PM-2.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Paraliobacillus.
OX NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR47247.1, ECO:0000313|Proteomes:UP000199066};
RN [1] {ECO:0000313|EMBL:CQR47247.1, ECO:0000313|Proteomes:UP000199066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM-2 {ECO:0000313|EMBL:CQR47247.1,
RC ECO:0000313|Proteomes:UP000199066};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000427};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor
CC {ECO:0000256|ARBA:ARBA00004168}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
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DR EMBL; CTEI01000001; CQR47247.1; -; Genomic_DNA.
DR RefSeq; WP_090855085.1; NZ_CTEI01000001.1.
DR AlphaFoldDB; A0A0U1KMM0; -.
DR STRING; 1462524.BN1058_01554; -.
DR OrthoDB; 7294637at2; -.
DR Proteomes; UP000199066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR GO; GO:0006689; P:ganglioside catabolic process; IEA:TreeGrafter.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 2.40.220.10; Intramolecular Trans-sialidase, Domain 3; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR004124; Glyco_hydro_33_N.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR023364; Trans_sialidase_dom3.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR10628:SF30; EXO-ALPHA-SIALIDASE; 1.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02973; Sialidase; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000199066};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1031
FT /note="exo-alpha-sialidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006710405"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 995..1031
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..982
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 114046 MW; 3F14EB27C08994A8 CRC64;
MYKIKNLFMI ICSIAVVLVN LSPSMEALAV EDSDLPEPIL RVENERIGDG YFTNLNENVD
DLKSLDEGTI IVRFRNTGSS IMSLFSLSNS DVRDGHFHMY VTPTTLGSEN RLEKPDTAKE
NIHVHSNAKL EVGAVHTVAM VVDKDKGYKY FVDGELIMED TQSPVKFLSN IYQPDSAQLG
RTDRAAGSNE YPFSGDIDFA EVYNQPLNDQ VLLDITGETD QEKKLNPLPE DALITEPDSV
FYPGFMDSNN YRIPALLYTE DNTLIAGIDR RVNHGGDSPA NIDAAVRRSF DQGDTWEEDG
IIVNNYPDQA SNIDLTLLQD KTNERIFALV DGFPQGGGFW SAKKGSGFKT IDGEKYMLLT
DEDGNEFTIR DNGVVYDASN NPTDYSVDQK RNLYLNDEKI DNVFSATTPL KAYLTSYLEL
YYSDDEGETW TGPIDLNDEV KEEWMSFLGT GPGNGIQLTQ GPNKGRLVMP VYFLNDAGKQ
ASAVVYSDDH GETWHRGESP NEGRDVGNGQ TINEKDFSNS SYEITEAQVV EMPDGQLKMF
MRNFSGYARI ATSFDGGETW HSEVVVEEDL VAPYSQMSAI RYNGQIDGKE AVIFSSAGNS
SQRINGKVRV GLIEEDGTYE NGETKYAFDW KYEQLVKEGH YGYSSLTNLE NGEIGLFYEA
TGNTNMDFIK FNPEFLKWKK YKDNEKPNLV SFEVTDNDKS LYKSGDTIKV EAQFDDYVML
MGEKQLVGTI GDKTIAFDLV EQNGSFVFEG TVPELEDNQY DMNVAFANQL DIYSVKGESF
EKDSESSTID TTIGIGVSPN SVEIDQSNVN LVEGGKTIQL STSVNPIDAT ILDLQWESTN
TDVATVDEDG IVTSVNPGTA TIKVTANGEF TDEITVTVEA LDVTALETII TTAENISNAD
GSYTEESFQA LQTAIADAKS AVESIETEED VTNAVAALQG AIDGLEEASE QDSDDNTDEN
GDSSNTEDEN ENSSNTEDEN GENQEQSSNG DDNELPNTAT PMYNWMLIGL LLITIASGLL
LYRRKTLLNR N
//
