ID A0A917AQH6_9BACI Unreviewed; 644 AA.
AC A0A917AQH6;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 11.
DE SubName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0000313|EMBL:GGE68211.1};
GN ORFNames=GCM10007140_17830 {ECO:0000313|EMBL:GGE68211.1};
OS Priestia taiwanensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1347902 {ECO:0000313|EMBL:GGE68211.1, ECO:0000313|Proteomes:UP000605259};
RN [1] {ECO:0000313|EMBL:GGE68211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.12698 {ECO:0000313|EMBL:GGE68211.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:GGE68211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.12698 {ECO:0000313|EMBL:GGE68211.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor
CC {ECO:0000256|ARBA:ARBA00004168}.
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:GGE68211.1}.
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DR EMBL; BMFK01000001; GGE68211.1; -; Genomic_DNA.
DR RefSeq; WP_188388011.1; NZ_BMFK01000001.1.
DR Proteomes; UP000605259; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:TreeGrafter.
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 PANTHER; PTHR11575:SF24; 5'-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.
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 Reference proteome {ECO:0000313|Proteomes:UP000605259};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362119};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 30..644
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5038159359"
FT TRANSMEM 618..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..274
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 361..508
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT DOMAIN 604..642
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 69822 MW; 09E441A84471EED5 CRC64;
MWKKPALSIA LATSLVVPTV LGTTDTIQAA EEPKYIDVQF LGINDFHGSI KNAAYLAGSF
NQREAEATAK GAHTIRVHAG DAVGASPAES SLLQDEPTMK ILDKMNFKVG ALGNHEFDEG
LGELKRLYSG AEQHPNVKEY TQGTNYKYDG ISKDFKHLAA NVIDKKTGQP VFDPYTVKEI
GGVEVGFIGV VTTETPSVVM PEFVKDYDFI SEADAINKYT KELKDKGVKA IVVLGHVGAE
TNKTTNVTTG EFADIAHKID DEVDILFAAH SHKYANGVVD GKLIVQSQSH AKAFADIDAK
IDPATKDFVK GEMKAEIVDV TKESVTPDAE IQKIVDEATE ITKKVAGKEI AKAGSANPVG
ERKPEGGESS LGNLITDGQR ILTGADFAIT NSGGIRDSLN PTKNEKGEDI FTWGSAYAVQ
PFGNQVKTYE LTGQQIKDAL NQQWQNPARD MFLQISGFKY TYTKTDKGTH VVDMFLPDGK
KMDLNQTYSV AMNEFLAGGG DAFTKFKEGR LIEGNKTDTE MFVDYITQLG QQGKTIAPTI
EGRIKEVKAG ETKPEPPTTG GETTNPEPPT TGEEGTKPKP PTTGEEGTKP EPPTTEETKD
TVKETTDEKE LPNTATNMYS MMAAGVATLL AGTVVFFRRR KQQQ
//
