ID   D3H7K8_STRM6            Unreviewed;      1907 AA.
AC   D3H7K8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN   Name=nanA {ECO:0000313|EMBL:CBJ21850.1};
GN   OrderedLocusNames=smi_0601 {ECO:0000313|EMBL:CBJ21850.1};
OS   Streptococcus mitis (strain B6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ21850.1, ECO:0000313|Proteomes:UP000008563};
RN   [1] {ECO:0000313|EMBL:CBJ21850.1, ECO:0000313|Proteomes:UP000008563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:CBJ21850.1,
RC   ECO:0000313|Proteomes:UP000008563};
RX   PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA   Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA   Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT   "The genome of Streptococcus mitis B6--what is a commensal?";
RL   PLoS ONE 5:E9426-E9426(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
CC       {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR   EMBL; FN568063; CBJ21850.1; -; Genomic_DNA.
DR   RefSeq; YP_003445718.1; NC_013853.1.
DR   STRING; 365659.smi_0601; -.
DR   CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   KEGG; smb:smi_0601; -.
DR   PATRIC; fig|365659.3.peg.571; -.
DR   eggNOG; COG4409; Bacteria.
DR   HOGENOM; CLU_002070_0_0_9; -.
DR   OrthoDB; 7294637at2; -.
DR   Proteomes; UP000008563; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR004124; Glyco_hydro_33_N.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   InterPro; IPR001254; Trypsin_dom.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF02973; Sialidase; 1.
DR   Pfam; PF13365; Trypsin_2; 2.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Glycosidase {ECO:0000313|EMBL:CBJ21850.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:CBJ21850.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004296}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1882..1902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1875..1907
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          714..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1681..1713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1847..1875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1851..1875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1907 AA;  207924 MW;  C05E0ECBEE197320 CRC64;
     MFIRLKGLGK FRKSKAYGLV GCLTLFAVLG LAAPELPVIG GGVAYADVIQ GGNDIKDVEV
     HSDAANGVAM TYTTYDSGNS GQQTASGSGV FVAPNVMVTA AHNYYEKKTE DGSAVLRGGD
     SAKSYVVMNS DTEKINKVPT SGSTEAVAKE SIHAYNEKDF GKSYGNDLAV VVTNKTVEAM
     TNGEDSPREL SKTEVATGDS IRMVGYPNDF STSNLSEENR NRLKDGKPYE VEGKVSTLNK
     ENGAVTYHTS ALGGFSGAPL FNDKGEVVGI HQHGTNTASE VEANRIGGGT IFTEKHKEWI
     RSMVDRYAIT GWYLDGTIRY YYDENHKALK NVEKEIDGAR YRFNDRGQAT LLSGVEKGRV
     LLRLEDVKGN RLIADKVVQT GEVDSPIVFN LRQDSDFNRL VGDSPNAKIV SYNNLPINKL
     VTDTSWSGDY VSKVALGNTV IKAVLDSVAP KTDFARTEVG KVDLSGTANL PKPSEIVKNA
     PNGEQNFQAT THILTPDGTG SATLIAPNLL LTVAHNFLTV NGSKVVTKSG KENTVYKATL
     PNGTSINFSD EEIAYWNRAE SVFGFKNDLA LVRLKEAVQG VTPVEVVKQS AKVAEGNTVS
     VYGFPDNKLS PVLDSKVVGT TDFGSGIEGI SYGGTKPGAS GGGLYNDKGV LIGVHQNGVV
     DNRSGGLVLS KEQLDWVRSY IEGQPKEPVY VKDKEVASSK QDLDKELAEK LASATDNGVE
     INKESLKEEK PTNQEGNSEN VPAEPNVEKG EKTENLPEEV ESADNVVLPP RDYFARDLKN
     VKTVFEKEDL ATNAGNGQRV DLAEALDKLK HLQNATIHME FKPDANAPQF YNLFSVSSDK
     NRDEYFSMSV NKGTAMVEAR GADGSHFYGS YSDAPLKVKP GKWNSVTFTV ERPKADQPNG
     QVRLYVNGVL SRTNTKSGRF IKDMPDVNKI QIGATRRANQ TMWGSNLQVR NLTIYDRALT
     SEEVGKRSQL FKVADLEVKL PESAKITEKK EVFVSGVNGG LNKDGINTYR IPALLKTDKG
     TLIAGADERR LQFADWGDIG MVVRRSQDGG ETWGDRITIS NLRDNPDAKD KTAPSPLNID
     MVLVQDPETK RIFSVYDMFP EGKAVFGMPA KPEKAYERIG DKTYQILYKT GEKGYYTIRE
     NGEVYNSKNQ KTDYHVVVNP KKLGYSDKGD LYKGKDLIGN VYFAQSTKNP FKVANTSYLW
     MSYSDDDGKT WSAPKDITPG IRQDWMKFLG TGPGTGIVLR TGEHKGRILV PAYTTNSVSH
     LGGSQSSRLI YSDDHGVTWH AGEAPNDNRP VGNKTIHSSN MNNGGAQNTE STVLQLNNGD
     VKLFMRGLTG DLQVATSKDG GITWEKTIKR YPEVKDAYVQ MSAIHTMHDG KEYILLSNAA
     GPGRERKDGL VHLARVEKNG ELTWIKHHLI QGGEFAYNSL QDLGNGEYGI LYEHSENGQN
     RYTLSYKKFN WDFLTKDRIS PKEVKVKQVS DMGEGIMSLE FDSEVLVNQA PTLSLANGKT
     IEFMTQLDNK TLLFAVNKKD IGQEITGIVG GSIESMHDLP VNLRNSGIPG GINSAEVAVN
     ELDDYTGAIG TAGEEIATTE SLLDYSGGVS SEPVVTPEVD EYSGGVNAVE AAASELDDYT
     GAIGTAGEEI ATAESLLDYS GGVSSEPVVT PEVDEYSGGV NAVEAAVNEL EDYTGLFATP
     EETSTVKSTE KQVSNKESKK EEKTNQVIPS LDSSQRLFKN ETGSVHIQAS EEVLRNVKAV
     QIEEVKVSSL SSLNYKAFDI KLKNADGQSV QPKGKVLITF TTDQSVENVY YVDPEGNLHP
     LEFTQKDGKV IFGTNHFSIY AMTFRLSVNN LALDNATKDK KEEEIAPLPK LLSTNQHSES
     NQSENRVSNN EQTMLPNTGE SASLLTILFG FVGVFLGAMI SYKRKDS
//