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Database: UniProt
Entry: F9PE30_9STRE
LinkDB: F9PE30_9STRE
Original site: F9PE30_9STRE 
ID   F9PE30_9STRE            Unreviewed;      2429 AA.
AC   F9PE30;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Gram-positive signal peptide protein, YSIRK family {ECO:0000313|EMBL:EGV13183.1};
GN   ORFNames=HMPREF1124_0309 {ECO:0000313|EMBL:EGV13183.1};
OS   Streptococcus infantis X.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=997830 {ECO:0000313|EMBL:EGV13183.1, ECO:0000313|Proteomes:UP000003399};
RN   [1] {ECO:0000313|EMBL:EGV13183.1, ECO:0000313|Proteomes:UP000003399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X {ECO:0000313|EMBL:EGV13183.1,
RC   ECO:0000313|Proteomes:UP000003399};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EGV13183.1}.
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DR   EMBL; AFUQ01000007; EGV13183.1; -; Genomic_DNA.
DR   PATRIC; fig|997830.4.peg.1069; -.
DR   eggNOG; COG3250; Bacteria.
DR   eggNOG; COG3583; Bacteria.
DR   Proteomes; UP000003399; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR049487; BgaA-like_CBM.
DR   InterPro; IPR011081; Big_4.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF21606; BgaA-like_CBM; 2.
DR   Pfam; PF07532; Big_4; 4.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01208; G5; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
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..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..2429
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003385246"
FT   DOMAIN          2138..2220
FT                   /note="G5"
FT                   /evidence="ECO:0000259|PROSITE:PS51109"
FT   DOMAIN          2396..2429
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          65..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2364..2401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2367..2388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2429 AA;  267233 MW;  122D800C6D4D79AC CRC64;
     MDKRFFEKRC HFSIRKFAIG AASVMIGASI FGLQVAQAAE TETSSTTEET IHQVQPLDKL
     PDDLAAAIAK AEQNGPQDSA TEKEEKDTDE AAKPVTEDKV TEETSPKKEK EVEVVSPKEE
     ITEKPAAEVN EKEPTVAEVN TEKPAVLEEH TAEANQNKPV SDDKAKEEKI SATDLPQVTK
     EKEKEDQLLQ ERKQNFNKDW YFKLNAQGDF SKKDVDVHDW SKLNLPHDWS IYFDFDHKSP
     ARNEGGQLNG GTAWYRKTFT VDEAAKDKDV RINFDGVYMD SKVYVNGKFV GHYPSGYNHF
     SYDITEFLNK DGSENTIAVQ VTNKQPSSRW YSGSGIYRDV TLSYRDKVQV AENGNHITTP
     KLAQQKDGNV ETQIQSKIKN TAKTLAKVFV EQQIFTKEGK AVSDLVRSVT KNLAGNEAAD
     FKQTILVNKP TLWTTKSYNP QLYVLKTKVY NEGQLVDVTE DTFGYRYFNW TAKEGFSLNG
     ERMKFHGVSI HHDNGALGAE ENYKATYRKL KLLKDMGVNS IRTTHNPASP QLLDAAASLG
     LLVQEEAFDT WYRGKKTYDY GRFFDQDATH PEAKKGEKWS DFDLRTMVER DKNNPSIIMW
     SLGNEVDEAD GGERSLETAK RLKAVIKAID TERYVTMGEN KFSRASTGLF LKLAAIMDAV
     GMNYGERFYD AVRKAHPDWL IYGSETSSAT RTRDSYFYPA KNLYHDNRPN RHYEQSDYGN
     DRVAWGRTAT ESWTFDRDRA GYAGQFIWTG FDYIGEPTPW HNQDHTPVKS SYFGIIDTAG
     LPKNDFYLYR SEWYSAKEKP TVRIMPHWNW TDETLKERNM LINGKVPVRT FSNAASVELF
     LNNESLGKKE FTKKTTADGR PYHEGANPGE LYLEWLVEYK PGTLTAIARD ENGKEIARDS
     VTTAGEPARV RLTKEEHVIT ADGKDLSYIH YEIVDEDGNV VPTANNLVHF NLHGQGQIVG
     VDNGEQASRE RYKAQKDGTW QRKAFNGKGV VIVKSTEKEG KFTLYADSAG LASDQATVTT
     VSGKKENRHF VAFAPVKATT DVSENPKLPK TVTAIYSDGS VEEKSVTWDI PDDLLTSAGE
     KKVLGSVEGL EAKAEALVKV IALDKWLPKV ATVPVGTATE DLDKTVTAVL SDGNLVDADV
     VSWTLKDPSA LTKEGGRTEA TGKLVGNDYE VTATFIASDQ ETENTVTGLT VGDKALADFE
     PGKTYYRVSL PYSAKIPSVG AQARGYQVTV QQASAANDYQ ASVFLSDQKG DLVQTYLIQF
     VKEAPALTRL EVSVEGKENA TEDQVLPYHV IGHYEDGSQT EFSASDIHLD ASSTDGGHLE
     VNGQNLLLYT KGSVTLTPRI EHQTEKTQSV ATVVVIKENK VAKKIVKLHP VSISTDINQQ
     PNLPDQIGAE FDKGLPRKLA VTWDKVDEKE LASYHSFTLK GHVEGTDIEA VANVTVEGLQ
     VAEEISLTLP KGETVQLPAN VRAYHSNGTT VYNDVVWDKV PANFSQTEGI FEIKGQLVGS
     SLTTKAHVRV SSQVVAGNNI SKQWTGSQLP AAIVSNTGGD DSANTLNDLT VSRANTDVKN
     RWTTWQTNTD NDWASILFGN SGDLTKRFVD NLSVDFYTDG AIGLPKEYVI EYYVGQEIPD
     LPTDVNHAQG DANHPFNNAA NWKEVEHLKA PGQLSASQTN HFTFDKVETY AVRIRMKKAN
     GTDGVGLTEI TILGNKVPSA TSSEISIRVD GQKLEHFNPA KTDYHIPQAS KVITATASDN
     GLVTIVPATS PEGATRLILK AEDGTILKEY RIFRDGQKES TQPVAAENAA MTLSVGDKLQ
     LPTEVTVYYP SETDWTRDKL AVEWDAVPEH ATDQEGTFEV LGHILGTDLT TKMQVTVLAR
     GNQVISENTS NNATDSKAFA STTNDTDAAS NDRIFYINDG RFNEDGRWTN WSRTPKNQEV
     SVGVLFKKNG QITPRSVGKV AIQFFKDSGT DAPATMVLER YVGPVYSEPS TISRYEENAD
     HPFNKAENWQ EIPYKASGAI EAGKPIEFTF DPIQTTAIRA RMTRKSTTNG LAMVEFSAYS
     PAKASDSETP AVTISVAGKA LENFDPAVSE YRLTANGAKP EVTVQTSGHG VATVVESNQG
     NLPTLVRLLA KDGSLVKEYR LHFEAGSEAS HAVDDQALVL DRPSLEVEKA VIPFKEIIRE
     NSDLAKDERR IVSVGQNGEK VDYVEVLGTS RKVVHTETIE AKDQIVEVGV KAVATSSKGE
     EPAPVLEIPE YTDPIGTVGE EPAPIVEVPE YSNSIGTAGD QAAPVLEVPE FKGGANWVEA
     ATNEVPEFKG GANWVEAAKN EVPEFKGGAN WVEAATNEVP EFKGGANAVQ ADKNELPEYT
     GTLGTAGDQA APTIDKPVAD IRGLSDKPSE TQASAEQTQV SQVLGNASEK AVSARLPETG
     ESQSDTAIFL AGLSLALSAA FLNGKRKEE
//
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