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Database: UniProt
Entry: G5JPI7_STRCG
LinkDB: G5JPI7_STRCG
Original site: G5JPI7_STRCG 
ID   G5JPI7_STRCG            Unreviewed;       697 AA.
AC   G5JPI7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=5'-nucleotidase family protein {ECO:0000313|EMBL:EHI75536.1};
GN   ORFNames=STRCR_1639 {ECO:0000313|EMBL:EHI75536.1};
OS   Streptococcus criceti HS-6.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI75536.1, ECO:0000313|Proteomes:UP000004322};
RN   [1] {ECO:0000313|EMBL:EHI75536.1, ECO:0000313|Proteomes:UP000004322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS-6 {ECO:0000313|EMBL:EHI75536.1,
RC   ECO:0000313|Proteomes:UP000004322};
RA   Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA   Town C.D.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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:EHI75536.1}.
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DR   EMBL; AEUV02000002; EHI75536.1; -; Genomic_DNA.
DR   RefSeq; WP_004230053.1; NZ_AEUV02000002.1.
DR   AlphaFoldDB; G5JPI7; -.
DR   STRING; 873449.STRCR_1639; -.
DR   eggNOG; COG0737; Bacteria.
DR   OrthoDB; 9801679at2; -.
DR   Proteomes; UP000004322; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Signal {ECO:0000256|RuleBase:RU362119}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT   CHAIN           28..697
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT                   /id="PRO_5005132433"
FT   DOMAIN          663..697
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          617..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  75562 MW;  E2B5D58C9FCEA60E CRC64;
     MKKHIFLKSS LLALVAGASF LSIQAAADQV DVQVLGVNDF HGALDTTGTA SMPDGPVRDA
     GGVAQLDAYM DDAQTQFQAE HPQGDTTRVQ AGDMVGASPA NSGLLQDEPT VKAFNQMDVQ
     FGTIGNHEFD EGLAEYNRIV QGQAPEPGKF DPIVDQYSAD GQQEAAKQQI LAANIIDQKT
     NQIPFGWQPY AIKTIPINGK KVKMGYIGIV TTEIPNLVLR KNLEGYTFLD EAETIAKYAK
     ELNDQGVHAI GVLAHVAADN DAGELEGDAV PILNKLNQIY PDNSVDIFFA GHSHKYANGV
     VGRTRVVQAT SQGKAFEDVR GVLDTDTGDF TDIPSAQIIP VAPGKAGSPD LQAIVDDASR
     RVKTVTQAKI GTATFPQAIT RETNQDKETA VGDLVTQGQL TIARKTYPDV DFALTNNGGV
     RSDLIVNPDK SITWGAAQAV QPFGNVLQVV QLTGQQIYDA LNQQYDEQQR YFFQMAGLHY
     LYTDNPAGGK ETPYKVVKAY KDDGSEIDPN QTYKVVINDF LYGGGDGFSV LRNAPLIGAI
     DPDTETFVQY IKDQEAAGKT VDIPEMNHKT YVTVQTAHTY QDRPDGRHLL TIETYVNRQG
     QPVGQAIISD QLIKENQSEA RAQRETQDLP SASFNLTPLA DKTGNQSTAA QAKQVKRTEA
     KSLPETGTEE KSATALSLVG LIMTFTVFFT GKKKEEN
//
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