ID F0FFU6_STRSA Unreviewed; 803 AA.
AC F0FFU6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative 2',3'-cyclic-nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:EGC22361.1};
DE EC=3.1.4.16 {ECO:0000313|EMBL:EGC22361.1};
GN Name=cpdB {ECO:0000313|EMBL:EGC22361.1};
GN ORFNames=HMPREF9388_1578 {ECO:0000313|EMBL:EGC22361.1};
OS Streptococcus sanguinis SK353.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC22361.1, ECO:0000313|Proteomes:UP000004185};
RN [1] {ECO:0000313|EMBL:EGC22361.1, ECO:0000313|Proteomes:UP000004185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK353 {ECO:0000313|EMBL:EGC22361.1,
RC ECO:0000313|Proteomes:UP000004185};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000527};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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:EGC22361.1}.
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DR EMBL; AEWY01000007; EGC22361.1; -; Genomic_DNA.
DR RefSeq; WP_002898555.1; NZ_GL872307.1.
DR AlphaFoldDB; F0FFU6; -.
DR PATRIC; fig|888815.3.peg.1550; -.
DR HOGENOM; CLU_005854_2_0_9; -.
DR Proteomes; UP000004185; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd07410; MPP_CpdB_N; 1.
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; IPR041827; CpdB_N.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 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 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000313|EMBL:EGC22361.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..803
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003252371"
FT TRANSMEM 780..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 771..803
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 41..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 86467 MW; 52F56830ABBAD364 CRC64;
MSKSSLQKTV VLLSAAALAA AVNAVQADEN TAAVTANPAA VESSAAEAKP TTAASSTEAT
ATPESTEPSS AISPENAGGN IDALMAMARN VAATEDTKPV EGQTVDVRIL ATTDLHTNLV
NYDYYQDKPV ETLGLAKTAV LIEKAKKENP NVLLVDNGDT IQGTPLGTYK AIVNPVEKGE
QHPMYAALQA LGFEAGTLGN HEFNYGLDYL NRVIETAGLP IVNANVLDPA TGKFIYQPYK
IIEKTFTDTQ GRLTTVKIGV TGIVPPQILN WDKANLEGKV VVRDSVEAIR DIIPEMRKAG
ADITLVLSHS GIGDDKYEKG EENEGYQIAS LPGVDAVVTG HSHAEFPSGN GTGFYEKYPG
VDGINGKING TPVTMAGKYG DHLGVIDLKL NYTDGKWKVT DSKGSIRKVD TKSNVADQRV
IDIAKESHQG TINYVRQQVG TTTAPITSYF SLVKDDPSVQ IVNNAQLWYA KQELAGTPEA
NLPILSAAAP FKAGTRGDAT AYTDIPAGPI AIKNVADLYL YDNVTAILKV NGAQLKEWLE
MSAGQFNTID PNNSQPQNLV NTDYRTYNFD VIDGVTYEFD ITQPNKYDRE GKLANPNASR
VRNLKYQGKE IDPNQEFIVV TNNYRSNGNF PGVREASLNR LLNLENRQAI INYILAVKNI
NPSADQNWHF ADTIKGLDLR FLTADKAKNL IGTDGDIVYL AASAQEGFGE YKFVYVAPKT
EPVPIEQSSS PTIAVEAANL QHSRVDFPVL TAVDPSTNKQ ASHRQAGAES LPATGEKTSS
LGLLGLVMTG LAGIFAFKKR ERQ
//
