ID A8AUR8_STRGC Unreviewed; 1582 AA.
AC A8AUR8;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=LPXTG cell wall surface protein, glycosyl hydrolase family {ECO:0000313|EMBL:ABV09481.1};
GN OrderedLocusNames=SGO_0208 {ECO:0000313|EMBL:ABV09481.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09481.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV09481.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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DR EMBL; CP000725; ABV09481.1; -; Genomic_DNA.
DR STRING; 467705.SGO_0208; -.
DR KEGG; sgo:SGO_0208; -.
DR eggNOG; COG3583; Bacteria.
DR eggNOG; COG4724; Bacteria.
DR HOGENOM; CLU_003704_0_0_9; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3630; -; 2.
DR Gene3D; 1.20.120.1850; Ebh helix bundles repeating unit (S and A modules); 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032979; ENGase.
DR InterPro; IPR005201; Glyco_hydro_85.
DR InterPro; IPR022038; Ig-like_bact.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR13246:SF1; CYTOSOLIC ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR13246; ENDO BETA N-ACETYLGLUCOSAMINIDASE; 1.
DR Pfam; PF07523; Big_3; 2.
DR Pfam; PF03644; Glyco_hydro_85; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABV09481.1};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1550..1582
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 55..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 174401 MW; 9E0CFEFFAF4A9CF9 CRC64;
MEFYKKQKFS IRKLSLGVCS VLVGIALFGV ADVSAEEKLT ELSQASDVAL VNADAPKEEA
AEEAQGKPAS EEASQAAQPD TENQAVVEDK KPVVESQDVA IVAEKEEKPA TKEAKVVEDL
PSQEDKKLKP KEVKFDNWQD LLNWKPGDRE DDDINRASVP LAERYQGHQI NQQANPEAKV
QALSNMNSKA LDHASTGGEE FKAYAFDYWQ YLHSMVFWDG LVPTSDVIDA AHRNGVPIYG
TLFFNWSSSA KDQERFAEAL KEDSEGSKTF PIARKLVELA KYYGYDGYFI NQETTGSQVE
PLGPKMRDFL LYTKEYARSL NYPIKYSWYD AMTYEYGRYH ENALGEYNYQ FMQPKDGENP
VDTFFANFNW GKAETDYSIS TAKWIKRNPY DVLAGIELQK GGSYKTNVDW EAILDENGKL
RLSLGLYAPD TITGLGKTGE GYHIHENYFW TGFQGDPSKG KPSDQSWYGM SNLVVDKTAI
TKPDFNTSFN TGHGKRWFVD GKVSKDGEWN YRSVSGFLPT WRWWIQHSEG SAPLKGRYDF
DEAYNGGNSL AFEGNLDANS SQNVMLYSTK IPVSDKTKLS LTHKGGQGTS AWVALATKPD
YSEYEWKELN PSKDWKTETF DLSSLAGKTI YGVKMFFDHD SDVKDYKFNL GQLSIYANQE
KPAAPKDVVV KAKRLQNAQE AEALLQFKGS ADADYYEIYE KDGDQWRLVT GTSGTSAYLA
KVTRSASAKG SKQELKVVAV GKNGLRSDAG TVDFDWGMQV SDTSLPKPLA PNVVLGAKVI
GSSFPDADGS EGIEGMLNGT ITSLSDKWSS AQLSGTVDIR LTQPRTVTRW VMEHAGAGGE
SVDDGKMNTR DFDLYYKDEA GEWKLAKAVR GNKDHVSDIV LDKPIRAQDW RLDVITADNG
TPWRAIRIYN WKMYESLDTE TVNVPMKNAA ARVLGNGHVQ VGFKDVAAKT TVSLYESSDA
KQAIATMTTD KDGNLIFKPL AFAKLPNLLY YRSQVEGKDI SNVLAIEVPK EDKEISKVEL
ETAPERKVYR QGDALSLKGG TIRVSFKGGE ANQLIQLSNS GVEVTGYDPS KLGEQHLQVS
YLGQKLDQSL TVYVVSHSEA GEKTPVGLEL IEKPKTDYIV GESLETQGGR FRLVFDDETT
EEHALDEAGV QVTGYDAHKE GRQTISISYR GVTTTYDVFV SPKPALNDEY LKQKLAEATA
VQNKVDFSFA SQGNKDALLK EIASAEQILK DHDTSTQGQV DESLSKLTQA FKALDGRKNF
ATKTSELDTL ATEAQDLLAQ NPNHPSGDAL LNLLNKNKDL LASSEVTPEA LETAKTSLQA
LIALLKEDKP AVFVDSATGV EVQFSNKETT PVKGLKVGVV EANAAEKEAF AGRLGKVYDI
EGVDKEGRDI DTQHASLVKI PVEAGKEVEQ VFFFPDNQPV QSLAFEQVGN EVIFTAPHFT
HYALVYKTAK ASGSDQALKP DQPSEPDKPT VPSNDNSKPL HPQLPGDGHL SPVQPNANPT
VERLNYQEKD KGSTGYQSQN LANSSSQSVK EEVDSKDVKE ENTVTSAGNL PNTASQETAF
VAEAVLLAAL GGLLLAGKKK ED
//