AP4AH_BACSU
ID AP4AH_BACSU Reviewed; 186 AA.
AC P54456;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000305};
DE EC=3.6.1.41 {ECO:0000250|UniProtKB:Q2G297};
DE AltName: Full=Ap4A hydrolase {ECO:0000305};
GN Name=yqeK; OrderedLocusNames=BSU25630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP ROLE IN FORMATION OF BIOFILMS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168, and 3610;
RX PubMed=15175311; DOI=10.1128/jb.186.12.3970-3979.2004;
RA Branda S.S., Gonzalez-Pastor J.E., Dervyn E., Ehrlich S.D., Losick R.,
RA Kolter R.;
RT "Genes involved in formation of structured multicellular communities by
RT Bacillus subtilis.";
RL J. Bacteriol. 186:3970-3979(2004).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=32152217; DOI=10.1128/jb.00053-20;
RA Minazzato G., Gasparrini M., Amici A., Cianci M., Mazzola F., Orsomando G.,
RA Sorci L., Raffaelli N.;
RT "Functional characterization of COG1713 (YqeK) as a novel diadenosine
RT tetraphosphate hydrolase family.";
RL J. Bacteriol. 202:e00053-e00053(2020).
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to
CC yield ADP. {ECO:0000250|UniProtKB:Q2G297}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2
CC H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41;
CC Evidence={ECO:0000250|UniProtKB:Q2G297};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2G297}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows increased levels of Ap4G, Ap4U, Ap3A
CC and Ap4A (PubMed:32152217). Cells form pellicles that are initially
CC flat and thin. The pellicles finally become thicker, their flat
CC surfaces are broken by a number of broad pits, the inner surface of
CC which are covered with fruiting bodies. The colonies also show a defect
CC in gross morphology, in that their central region is flat ang glossy
CC (PubMed:15175311). {ECO:0000269|PubMed:15175311,
CC ECO:0000269|PubMed:32152217}.
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase YqeK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84432; BAA12448.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14505.1; -; Genomic_DNA.
DR PIR; G69951; G69951.
DR RefSeq; NP_390441.1; NC_000964.3.
DR RefSeq; WP_004399059.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54456; -.
DR SMR; P54456; -.
DR STRING; 224308.BSU25630; -.
DR PaxDb; P54456; -.
DR PRIDE; P54456; -.
DR EnsemblBacteria; CAB14505; CAB14505; BSU_25630.
DR GeneID; 937831; -.
DR KEGG; bsu:BSU25630; -.
DR PATRIC; fig|224308.179.peg.2786; -.
DR eggNOG; COG1713; Bacteria.
DR InParanoid; P54456; -.
DR OMA; ILTRNWA; -.
DR PhylomeDB; P54456; -.
DR BioCyc; BSUB:BSU25630-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR005249; YqeK.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR00488; TIGR00488; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Iron; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..186
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000049786"
FT DOMAIN 18..132
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 21
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 51..54
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 83
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 109..110
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 127
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 133
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
FT BINDING 170..175
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9KD90"
SQ SEQUENCE 186 AA; 21282 MW; 2221986EC9797D29 CRC64;
MNREEALACV KQQLTEHRYI HTVGVMNTAI ELAERFGADS KKAEIAAIFH DYAKFRPKEE
MKQIIAREKM PAHLLDHNPE LWHAPVGAYL VQREAGVQDE DILDAIRYHT SGRPGMTLLE
KVIYVADYIE PNRAFPGVDE VRKLAETDLN QALIQSIKNT MVFLMKKNQP VFPDTFLTYN
WLVSGS
