ID E6KKT5_STROR Unreviewed; 2759 AA.
AC E6KKT5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Gram-positive signal peptide protein, YSIRK family {ECO:0000313|EMBL:EFU63577.1};
GN ORFNames=HMPREF8578_0850 {ECO:0000313|EMBL:EFU63577.1};
OS Streptococcus oralis ATCC 49296.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888049 {ECO:0000313|EMBL:EFU63577.1, ECO:0000313|Proteomes:UP000004500};
RN [1] {ECO:0000313|EMBL:EFU63577.1, ECO:0000313|Proteomes:UP000004500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49296 {ECO:0000313|EMBL:EFU63577.1,
RC ECO:0000313|Proteomes:UP000004500};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (NOV-2010) 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:EFU63577.1}.
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DR EMBL; AEPO01000010; EFU63577.1; -; Genomic_DNA.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_227792_0_0_9; -.
DR Proteomes; UP000004500; 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; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 5.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR019931; LPXTG_anchor.
DR InterPro; IPR011496; O-GlcNAcase_cat.
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; PF00754; F5_F8_type_C; 5.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 2.
DR Pfam; PF07555; NAGidase; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 5.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 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}.
FT DOMAIN 1056..1164
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2012..2159
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2327..2435
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2727..2759
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 79..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2704..2734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 711
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 2759 AA; 305609 MW; E7B62E677CF8434A CRC64;
MYADERNRRK MDRHFFEKRC HYSIRKFAIG AASVMIGASI FGANMVQAAE TATPSETEGS
ITHVQALDKL PDDLAAALEK ADAEAATEAS HEETPATDEG TNPAASEETK PETSPASPKP
AETPKPVETP KADKQPAETP TPAVKPAEKT IEDREDVNHL EGATAQASNH ETGTNFTADK
AIDGDDNTRW ATDRDAVKPT FELTLPKTTL IKHVEIDWDR RLRNGQNDPN IKSWSLYYAG
QEDVGANGEK QWKLAHTKTG DPVLDEKVDL ANSIQAKYLK LEINDYQAGT MGWRNVGIQE
IRAYSNVPDH SKVTDIRQVT ELTVAEDGQS LVLPTLPGKV SLIGSNKQGV IDLQNHIYKP
LTDQRVKVMV QQIRDSHTFT KEFEVVIKGL HQDEGVGVKP KVAPAVQQWY GKEGQSSITS
DTVLATGDSG FDQAATFYQS DLASRGLELA TGDKQAQKRI EFKKVENKGY GKEGYGITIQ
NDVITIEAAT NTGAFYATRT LLQMGETDLQ NGEIRDFPSF SHRGFMLDTG RKFIPYDTLV
DIMLNMAYYK MNDLQLHLND NYIFLKEHLA GKSLTPEEQL KYVLEHAKTG FRVETDIVGK
NGQKLTSDEH YTKEEMQNLI KLAKALHINL VPEIDTPGHA LSFVKVRPDL MYQGSLSDYA
GKHNVERVAM LDLDNKYEET LKFVKSVYDK LLDGPDAPLH GVSTVHIGTD EYYGSRESYR
RYVNDLTQYI KSKGYTPRIW GSLSAKRGNT PVDWNGVEVD IWSIGWQRPN EAIAQGAKII
NITDVPTYSV PSGSNSQAAY GDYANYERQY NSWTPNDFRT GGGPLLPASH PSILGGGHAV
WNDNIDLHET GLTSYDIFKR FFKSMQTTAE RTWGSDRAAA TFAERTLPTS PYAPQSNPDK
EIDQSDLFTI NPETVKNYAS KKVKTSEQGL AFEKDSSIEG LAGDVGPSHV LKFDVTVTGD
GEQTFSTSGD NRIYLADKDG YLAYQFEQFH IQFNKKLEKN KRYQISIVTK PQSTEVYVDG
EKIERIANPA HPRFAHNSLV LPLESIGGFK GILHSAELSD KPFVNPRLIS NDKITATASS
QQLPGNATEG AVEKAFDNDP NTFWHTKWTG DTGPYTLTMT LKEAEKVNGL TYLPRPGGGN
GVVTRYEIYA QKDGQMVKVS EGSWDNNAQE KTVNFTAVHT NKIELKVLEG VGGFASAAEV
HLLKPVKEEQ ETPAPSQPEK PTTPEKPKVE QTGDGTVELA DQFTASKPAS EDSIAAASKS
ADYLKKEYKV FPTPQKVTYG EGVTALRKQV NLVMGDQLDI YTRNRLKSVL QDNQVSYTTG
KAAIAGATNI YLGVHGQGSQ AEQNLSNVSA GLFDKIDAYV LSIKDNSISI VGKDTDAVFY
GLTTLKHMLK ESQVPVLRNV TVEDYAELKN RGFIEGYYGN PWSNADRAEL MRYGGDLKLN
QYFFAPKDDP YHNKKWRELY PEEKLAEIRE LARVGNQSKT RYVWTIHPFM NNRIRFGNEA
HYQEDLATIK AKFTQLMKVG VREFGILADD APSPVGGYNS YNRLMQDMTK WLTEMQGTYS
GLRKEMIFVP GQYWGNGRED ELKSLNENLP SSTSMTLTGG KIWGEVSESF LSTLKNNLSA
GGKTYRPVSL WINWPVTDNS KQHLILGGGE KFLHPNVDPS LLSGIMLNPM QQSEPSKIAL
FSGAQYSWKQ WKSEEEAKKI NDIAFNFVEN GHFEDSKVSA AFRELGKHMI NQNMDNRVVK
LEESVDLAPK LTDFMTKLKA GQDVTAERAA LRAEFAKIKE AAELYKASGD KKMVAQIHYW
LDNAIDQMNA LDAFLTGTEA MATNDAAKLW NSYYKGLKLY EQSQTHTFHY VDHMEKAELG
VQHIRPFILS LKEVLASEVQ KVLHPDQIIS TFITNRTGVE GGLAEVTDGD LATHAIIKSP
NSIKTGDYIG MKFNKPVSIQ TLTFAMGTQA NPNDTFSKAE VQYLDENDNW VTLKEPSYVG
NESLLKFENL NIKAKAVRMI ATADRENTWF AVQEIAVNRP VEKARSQQAT TVSLSSNLVY
KLNTSARQIT DGKDNTEAMM ANADGSNTTP VDAWAQLDLG EVKSVTKVRL RQGTGDKLAA
GVLEYSTDGT AWQELDRLSG EQTKEVTRAI NARYIRVRNT KALDLWWRIQ DFSVETRSGN
SELTDTNVDS LKETPVVDSL GSYELQIPSG TKLPAHSYLG MKLDRIHQIK SIQLKGQANP
ALTLEYSANA QEWTPASQLT DRTVATHLVR YVRLVNKTDQ EQAVTATSLL VTTKEVQPTK
LESTTMGIHP TYGSNDVRKL NNLDQLFDGV YNNFVEFSDY ARKDGHVTLK LGSERTIKKI
RAYIQDGTQN YLRDGKIQVS QDGKTWTDVV TVGDGVANST HDDSLTDGWT HDSKMPGNRY
IEGELTTPVK ANYLRVLYTA DYDARFVGFT ELVINDGEFV KPINDPTVEG SSGESQGNLY
NNLVDGKVLT SYKSEKDKGE LVYHLSEPTN ANHLRLVSSL PEGAKARILA RTLKDGQDSW
TDLGAITSSL QTFAIRNGGS LLDVKLVWEG GKAEFYELAS FHQELTEEPL QSSKGEEPAP
VLEVPEFTGG VNAVEALVHE LPEYTGPVAT VGDQAAPTVE KPEFKGGVNA VEALVHELPE
YTGPVATVGD QTAPTVEKPE FNGGVNAVMA LVHELPEYTG PLSTVGDQAA PTVEKPEFKL
STLVSDQGKT PDHKQEIARQ ETAKQSLPAT GESQSDTALF LAGVSLALSA LFVAKTKKD
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