ID R0MAI4_STRMT Unreviewed; 2136 AA.
AC R0MAI4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Cell wall surface anchor family protein {ECO:0000313|EMBL:EOB31996.1};
GN ORFNames=D065_07430 {ECO:0000313|EMBL:EOB31996.1};
OS Streptococcus mitis 13/39.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1239793 {ECO:0000313|EMBL:EOB31996.1, ECO:0000313|Proteomes:UP000013315};
RN [1] {ECO:0000313|EMBL:EOB31996.1, ECO:0000313|Proteomes:UP000013315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13/39 {ECO:0000313|EMBL:EOB31996.1,
RC ECO:0000313|Proteomes:UP000013315};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Semashko T.A.,
RA Karpova I.Y.U., Larin A.K., Ischenko D.S., Alekseev D.G., Klimova E.A.,
RA Filimonova A.V., Savinova T.A., Filimonova O.Y.U., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOB31996.1}.
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DR EMBL; AQTU01000020; EOB31996.1; -; Genomic_DNA.
DR PATRIC; fig|1239793.3.peg.1456; -.
DR Proteomes; UP000013315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 2.60.40.2030; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 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; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
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; IPR019931; LPXTG_anchor.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
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; 2.
DR Pfam; PF00746; Gram_pos_anchor; 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; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51109; G5; 2.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..2136
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004344642"
FT DOMAIN 966..1103
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1863..1944
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1975..2056
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT REGION 44..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2073..2107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2075..2107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2136 AA; 236305 MW; 1F6E114034BEBD8E CRC64;
MNRYLFEKEQ TFSIRKLTVG VASVMVGLAF FASGTALADE AKIETTSSQP NVEKLAEAEK
TKPEVKNESP VISTPQESEK AEKTVKSVEE KTVAETKTTD LLPEEIHDQA YPDAPVKNID
TSAIVDKKDS PKVETESILK NKEELPKEAE NGNRAIINGG LDLKHVPYEG QPATAASMIY
TIYNGGSQRY IVSGSGIFVA PNVILTVAHN FLESNRDTKE GHIRGGDSAK FYYNLGSNSA
VRNSQPVTGN TTLFKEEDIH FWNKKEFGKG YQNDLAAVVA PVPLQIASPN KAATFVPLAE
NKTYQPGDPV STIGYPTDSS SPELKKPIVA GQLYKADGVV KSVDNYDDKG SKGITYHMTS
VSGLSGAGII NGDGKVVGVH QHGTIENGIP DKDRFGGGIV LSPEQVKWVK DIIAKYGIKG
WYQGDNGKRY YFTPEGEMFR NKTAVIGENQ YSFDENGVAT LIKGIDYGRV VVQHVDETGN
PIKTDDTFVE KTEVGTAFDY DFKKEIAKTD FYTKNQEKYQ IVSIDGVEIN KQLKDEWTYN
VVSKTAPGTR VIKVVYKVNK GSFAIHYRLK GSEQELADVV TDNNDGKEYD VSFVNTFEAK
EIAGYRAITP RLEAIIQHEG VNDVVFEYEK ISDSSNPTST VLPAAHPEDK ETEIGNHGPL
PSKAQLDYHK EELAAFIHYG MNTYTNSEWG HGNEDPGYFN PTNLDTDQWI RTLKETGFKR
TIMVVKHHDG FVIYPSKYTN HTVAASPWKD GKGDLLEEVS KSATKYDMNM GVYLSPWDVN
SPKYKVDTEK EYNEYYLNQL KEILGNPKYG NKGKFIEVWM DGARGSGAQK VTYTFDEWFK
YIKEAEGDIA IFSAQPTSIR WIGNERGIAG DPVWHKVKKA NITENVKNEY LNHGDPDGDM
YSVGEADVSI RSGWFYHDNQ QPKSLKELMD IYFKSVGRGT PLLLNIPPNK EGKFADADVA
RLKEFKATLD QMYATDFAKG ATVTASSTRQ NHLYKESHLT DGKDDTSWAL SNDATTGSFT
VDLGQKRRFD VVELKEDIAK GQRISGFKIE VEINGRWVTY GEGSTVGYRR LIQGKPVEAQ
KIRVTITGAQ ATPILTNFSV YKTPSSIEKT DGYPLGLEYH SNTTADTAGT TWYNESEGVR
GTSMWTNQKD AKVSYTFTGT KAYVVSTVDP GHGEMSVYVD GQKVADVQTK NTSRKRSQKV
YETDDLAPGQ HTITLVNKTG EPIATEGIYT LNNNSKGMFE LEATSYEVEK GKPVTVKIKR
VGGSKGTATV RFITEPGTGV HGKVYQDTTQ DVTFEDGETE KTVTIPTIDF TEQADSIFDF
KAKLTSVTDG ALLGFATDAT IQVMKAELLI KDQTSYDDQA SQLDYSPGWH HETNSADKYQ
KTESWASFGR LTDEQKKKTT VTAYFYGTGL DIKGYVDPNH GIYKVFLDGK EVPYQEGMGN
ASTIEGKKYF SGHAAQRQGN QTLVSLKGLD ENLHAVTLQL DSDRNDLSRN IGIQVDQFIT
RGEGSELYSK TQILQSLSKW KDDLSNFDPS GLKNTATARQ AFKSNLDKLT AQLSSDTVNV
QDVMSTVTAL QDILSKNENY QKPGDETSPE QPVEPKQPEQ PEINYDKAMA SLTEAIEKKV
AELGANNDAK KKLVEITDKA IAAIQEAKTQ EDVNKALNNA LEQIKQLQPS QPEQPVEPKQ
PEQPEINYDK AMASLTEAIE KKVAELGTNN DAKKKLVEIT DKAIAAIQEA KTQEDVNKAL
NNALEQIKQL QPSQPEQPVE PKQPEQPKIN YDKAMASLTE AIEKKVAELG TNNDAKKKLV
EITDKAIAAI QEAKTQEDVN KALNNALEQI KQLQPSQPEQ PVEPKQPEKP ITSSSPEEGV
KELVFQLPSL DIVKKVLPFK TIRRENPQLD KGKEQVLAEG KDGAIIEYVE VDGSNRKVIQ
TESTPALDRV IEVGTKESSV GTDTPPVVTL PEYLLPKEPE KPITSSSPEE GVKDLVFKLP
SLDIVKKAVP FKTIRHENPN LDKGKEKVLA EGKDGLLIEY VEVDGSNRKV VQTKSTPALD
RIIEVGTKQS SVGTVAPPVV TLPEYVLPRE TEKPAPAVVT EDSPRKDEKA PVATTVRQDK
EKQLPETGEQ EANAFLFLAA ITSVLSLLIF QKNFKD
//
