ID J7TJE2_9STRE Unreviewed; 1343 AA.
AC J7TJE2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Gram-positive signal peptide protein, YSIRK family {ECO:0000313|EMBL:EJO17726.1};
GN ORFNames=HMPREF1149_0984 {ECO:0000313|EMBL:EJO17726.1};
OS Streptococcus sp. BS35b.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1105032 {ECO:0000313|EMBL:EJO17726.1, ECO:0000313|Proteomes:UP000006989};
RN [1] {ECO:0000313|EMBL:EJO17726.1, ECO:0000313|Proteomes:UP000006989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS35b {ECO:0000313|EMBL:EJO17726.1,
RC ECO:0000313|Proteomes:UP000006989};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:EJO17726.1}.
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DR EMBL; ALKH01000016; EJO17726.1; -; Genomic_DNA.
DR RefSeq; WP_000764178.1; NZ_ALKH01000016.1.
DR PATRIC; fig|1105032.3.peg.1674; -.
DR Proteomes; UP000006989; Unassembled WGS sequence.
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; 3.
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; 3.
DR Pfam; PF00728; Glyco_hydro_20; 2.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM01208; G5; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR PROSITE; PS51109; G5; 3.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1343
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003797338"
FT DOMAIN 1031..1110
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1122..1202
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1214..1294
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1312..1343
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 43..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 147620 MW; 47904F7A7A619E22 CRC64;
MKLEKKQRFS IRKYAVGAAS VLIGFAFSAQ VVSADGITPA PTAEETVQTI QESPQAVKEA
VGSKVPEKLE EKADKPVKEE VKEDQEAPRT VAPKTEESST PVVTENAAPT PTAEKESPAP
AETPAESTPS EKKNEAVTPA VATPSTERVS QVNEKLAKRK MISIDAGRKY FSPEQLKEII
DKAKHYGYTD LHLLVGNDGM RFMLDDMTIK ANGKTYASDD VKRALENGTD AYYKDPNGNH
LTESQMTDLI NYAKNKGIGL IPTVNSPGHM DAILHAMKEL GIQKPNFNYF GKESARTVDL
DNKEAVAFTK ALIDKYAAYF AGKSDIFNIG LDEYANDATD AKGWSVLQAD KYYPNEGYPV
GGYEKFIAYA NDLASIVKSH GLKPMAFNDG IYYNSDTSFG TFDKDIIVSM WTGGWGGYDV
ASSKLLVEKG HQILNTNDAW YYVFGRNADG QGWYNLDQGL NGIKNTPITS VPKSDGADIP
FIGGMVAAWA DTPSARYSPS RLFKLMRSFA NANAEYFAAD YESAEQALKE VPTDLKRYTA
ESVAAVKEAE KAIRSLDSNL SRAQQDTIDQ AIAKLQEAVN NLTFTPEAQK EEDAKREVEK
LAKNKVISID AGRKYFTLDQ LKRIVDKASE LGYSDVHLLL GNDGLRFLLD DMTITANGKT
YASDDVKKAI IEGTKAYYDD PNGTTLSQAE ITELIEYAKS KGLGLIPAIN SPGHMDAMLV
AMEKLGIKNP QANFDKVSKT TMDLENEEAM NFVKALIGKY MDFFAGKTKI FNYGTDEYAN
DATNAQGWYY LKWYGLYGKF AEYSNTLAAM AKERGLQPMA FNDGFYYEDK DDVEFDKDVI
ISYWSKGWWG YNLATPQYLA SKGYKLLNTN GDWYYVLGNH KPDEAYPLSK ALENSGKVPF
NQLASTKYPE VDLPTVGSML AIWADKPSAE YKEEEIFELM TAFADHNKDY FRANYNALRE
ELAQIPASLD GYSKESLDAL NAAKEALNYN LNRNKQAELD ALVAKLKAAR LGLKPAATYS
GSLDENELAA NVETKPELIT RAEKIPFEVI KKENPNLPAG QEKIITPGVE GERTHYISVL
TENGKQTETV LDSQVTKEPV TQVVEIGAPI THKGDEHGLA PAAETKPRLD IQEEEIPFTT
VTRENPLLLK GKTQVLTKGI NGRRSHYYSV STTADSKEVK TLVDSLVTQE AVTQVIEVGT
LVTHVGDEHG LAPAAEEKPR LDIQEEEIPF TTVTRENPQL PKGQSQVVVT GVNGRRTIFY
SVSTTADGKE ERTLVNSAVS QEAVAQVVEV GTAVEKAEQA EPTASKAEEK QLPATGSQDS
AGLVAAGLLA TLAAYGLTKR KED
//