ID F2QH03_STROU Unreviewed; 2064 AA.
AC F2QH03;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Cell wall surface anchor family protein {ECO:0000313|EMBL:CBZ00014.1};
GN OrderedLocusNames=SOR_0328 {ECO:0000313|EMBL:CBZ00014.1};
OS Streptococcus oralis (strain Uo5).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=927666 {ECO:0000313|EMBL:CBZ00014.1, ECO:0000313|Proteomes:UP000008131};
RN [1] {ECO:0000313|EMBL:CBZ00014.1, ECO:0000313|Proteomes:UP000008131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uo5 {ECO:0000313|EMBL:CBZ00014.1,
RC ECO:0000313|Proteomes:UP000008131};
RX PubMed=21460080; DOI=10.1128/JB.00321-11;
RA Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., Maurer P.,
RA Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT "Genome of Streptococcus oralis strain Uo5.";
RL J. Bacteriol. 193:2888-2889(2011).
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; FR720602; CBZ00014.1; -; Genomic_DNA.
DR RefSeq; WP_001083127.1; NC_015291.1.
DR KEGG; sor:SOR_0328; -.
DR eggNOG; COG1572; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_001189_0_1_9; -.
DR Proteomes; UP000008131; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.10.270.20; -; 1.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07501; G5; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00237; Calx_beta; 1.
DR SMART; SM01208; G5; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51170; CW; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51109; G5; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2040..2058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 407..427
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 957..1094
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1904..1985
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT REGION 63..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2000..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2064 AA; 228286 MW; BCE9D2DF48E14F75 CRC64;
MNRYLFEKGQ TFSIRKLTVG VASVIVGLAF FASGTVRADE TSPTTTSNFD KQIEQVADIE
EAKAEPVKEE GRVEAEKQET PAADTSSADL LPEEIQDRAY PDTPVKELDT TTIVDQKASP
KVETKSILKD KEEAPKEAEN GNRAIINGGQ DLKHINYEGQ PATAATMVYS TYNAGEQRYL
VSGSGIFVAP NLILTVAHNF LEANKETGEG HIRGGKSAQF YYNVGSNSEK KNSLPSSGTT
VLFREKDIHF WNKKEFGKGY KNDLALVEAP IPLPIASPNK AATFAPLAEH KTHQPGEAIS
TIGYPTDSSS KELKQPILAG QLYKADGTIR SVESYDDKGT TGITYKTTSV SGLSGGGIVD
SQGKVLGVHQ HGTVDNGVAE KDRFGGGLVL SPEQLKWVRD MIAKYGVKGW YQGDNGNRYY
FTDEGRMLRN EKAVIGSNEY SFNQDGIATL TKGVEYGRVV IQHEDEEGNP VKDNDTFIEQ
TAVDSPFDYN FKKEIEQTDF YQKNKDKYEI VSIDGVAVNK QLKDAWTEEH NVVSKAPAGT
RIIKVVYKVN KGSFKVYYRQ KGTTTELAEA TVDNNDGQEY EVSFVNTFHA KDITGYRPVK
TSLEARIQQK GVNEVVFEYE PIADTSNPTT PTPPVAHPED KETEIGNHGP LPSKAQLDYH
KEELAAFIHY GMNTYTNSEW GNGKEDPRYF NPTNLDTDQW IRTLKETGFK RTIMVVKHHD
GFVAYPSKYT DHTVAASPWK DGKGDLLEEV SKSASKYDMN MGVYLSPWDA NHPKYHVATE
KEYNEYYLNQ LKEILGNPKY GNKGKFIEVW MDGARGSGAQ KVTYTFDEWF KYIKEAEGDI
AIFSAQPTSV RWIGNERGIA GDPVWHKVKR ANITDDVKNE YLNHGDPDGD MYSVGEADVS
IRSGWFYHDN QQPKSLKELM DIYFKSVGRG TPLLLNIPPN KEGKFADADV ARLKEFKATL
DQMYATDFAK GATVTASSTR QNHLYKESHL TDGKDDTSWA LSNDATTGSF TVDLGQKRRF
DVVELKEDIA KGQRISGFKI EVEINGRWVP YGEGSTVGYR RLIQGQPVEA QKIRVTITGA
QATPILNNFS VYKTPSSIEK TDGYPLGLEY HSNTTADKAG TTWYNESEGV RGTSMWTNQK
DAKVSYTFTG TKAYVVSTVD PGHGEMSVYV DGQKVADVQT KNTSRKRSQK VFETGDLAPG
QHTITLVNKT GEPIATEGIY TLNNDSKGMF ELESTNYEVE KGKPVTVKIK RVGGSKGAAT
VRFITEPGTG VHGKVYQDTT QDVTFKDGET EKTVTIPTID FTEQADSIFD FKAKLTSVSD
GALLGFATDA TIQVMKAELL IKDQTSYDDQ ASQLDYSPGW HHETNSADKY QKTESWASFG
RLTDEQKKKT TVTAYFYGTG LDIKGYVDPN HGIYKVFLDG KEVPYQEGMG NASTIEGKKY
FSGHSAQRQG NQTLVSLKGL DENLHAVTLQ LDPDRNDLSR NIGIQVDQFI TRGEGSELYS
KADIIQSISK WKDDLSNFDP AGLKNTATAR QAFQANLEKL RNQLSADAVD VQDVMLTVSA
LQDILSKDEN YQRGQEEPSP EQPEQPEEPE KPEKPAQPEK PAEPKQPEIE YDKAMDSLTK
AIEKKVAELG SNKEAKKKLL EIADQAIAAI QEAKTQEAVN KALETALEQI NKLEAAQPEK
PAEPEKPVQP ENPTQPENPV QPEKPGQPEK PAQPEKPTQP ETPAQPEKPA QPEKPAQPEK
PAQPEKPTQP ENPVQPEKPA QPETPTQPET PAQPEKPTQP ETPAQPEKPT QPEKPAEPEK
PAQPEKPVQP ENPTQPEQPA QPETPAQPDN PVQPEKPAEP EKPAQPEKPV QPETPAQPEK
PVQPETPAQP EKPAQPETPA QPEKPAQPEK PITSSSPEEG VKDLVFTLPS LEIVNKVVPF
KTIRRENPQL DKGKEQVLSE GKDGLLVEYV EVDGDNRKIL QTEATPAQDR VIEVGSKQSS
VGTEAPPVVT LPEYVLPRET EKPAPVVTNN SSSKDEKAPV TATIKEDKER RLPATGEQEA
SAFLFLAAIT SILSLLIFQK NFKD
//
