ID I2J259_9STRE Unreviewed; 744 AA.
AC I2J259;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Gram positive anchor {ECO:0000313|EMBL:EIF37061.1};
GN ORFNames=HMPREF1116_0455 {ECO:0000313|EMBL:EIF37061.1};
OS Streptococcus sp. SK140.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1095726 {ECO:0000313|EMBL:EIF37061.1, ECO:0000313|Proteomes:UP000003237};
RN [1] {ECO:0000313|EMBL:EIF37061.1, ECO:0000313|Proteomes:UP000003237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK140 {ECO:0000313|EMBL:EIF37061.1,
RC ECO:0000313|Proteomes:UP000003237};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (APR-2012) 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:EIF37061.1}.
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DR EMBL; AJML01000037; EIF37061.1; -; Genomic_DNA.
DR AlphaFoldDB; I2J259; -.
DR PATRIC; fig|1095726.3.peg.1397; -.
DR eggNOG; COG0737; Bacteria.
DR Proteomes; UP000003237; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
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; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; NF040549; Nt5e_LPXTG; 1.
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 Pfam; PF00149; Metallophos; 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; PS00786; 5_NUCLEOTIDASE_2; 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 Membrane {ECO:0000256|SAM:Phobius};
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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 38..744
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5003661120"
FT TRANSMEM 721..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 713..744
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 597..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 80326 MW; CFA73136C6D2FB4A CRC64;
MVEERRERDF NMNKRFLLPV LSTALLAPAF LAGQVYAEEN TSSSEATEVV STTEAPVVTA
TPEVVTSPAT PVEEAAPQKE EADTVILHTN DVHGRIVEEK GVIGDAKLAT VIEKEREKGN
QTTLVVDAGD AFQGLPISNS TKGEARAKIL NEMGYDAMAV GNHEFDFGLD EVKKYKEILN
FPLLSSNTYV NGARLFEAAT IVDKNKDVAG DEFVVIGVTT PETATKTHPK NVKGVTFTEP
IAEVNKVIEE IQAKALAEGK DYKHYVVLAH LGVDTTTPVE WRGSTLAEAL SKNPLLKGKR
VTVIDGHSHT VESTTYGDNV TYNQTGSYLH NVGKITYKSR QLLGNPSLIA AADAKKLEAN
PKIEKLVKDI KQKYDAENAI EVVSNSPVEL NGDRENVRVR ETNLGNVVAD SLYQYGQTGF
SHPTDIAVTN GGGLRETIAK DKPITKGNVI AVLPFGNTIS QIQVTGQQVF DMFEKSLGSI
LQVDKAGKTV LDENGQPLLE PSGGFLQISG AKVYYDTNLA AGKRVLAIQV KNGATGLYEK
LDLEKVYYLA TNDFLAAGGD GYTMLGGARE EGPSMDAAFE DYLKTADLTQ YEKVNPNSRT
ISVDSKTFKL PEDQGKEQDP AKPGKDSETD PAKTPTQPGK NQETTPANSG NDATKPGKVQ
KTTPAKSEQD SATKTTPSGK NQGTTPAQTS TVKVDYKVAD QFANKTVVSE KLLPNTGSEQ
SIFMMLLGMI LGATALWTSR KQEK
//
