ID   A0LSA9_ACIC1            Unreviewed;       451 AA.
AC   A0LSA9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:ABK52319.1};
GN   OrderedLocusNames=Acel_0546 {ECO:0000313|EMBL:ABK52319.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52319.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52319.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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DR   EMBL; CP000481; ABK52319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LSA9; -.
DR   STRING; 351607.Acel_0546; -.
DR   KEGG; ace:Acel_0546; -.
DR   eggNOG; COG2206; Bacteria.
DR   HOGENOM; CLU_000445_92_14_11; -.
DR   InParanoid; A0LSA9; -.
DR   OrthoDB; 9802066at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   InterPro; IPR048430; MASE9.
DR   PANTHER; PTHR43155; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108-RELATED; 1.
DR   PANTHER; PTHR43155:SF8; METAL DEPENDENT PHOSPHOHYDROLASE; 1.
DR   Pfam; PF13487; HD_5; 1.
DR   Pfam; PF20972; MASE9; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABK52319.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        64..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..420
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000259|PROSITE:PS51832"
FT   DOMAIN          247..369
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   451 AA;  48056 MW;  EDEA18A5F51EC1F7 CRC64;
     MRSLPRAAAL YTSAMLLAGG LICAQALLHI RSSWSLVVPL VAICWIGEIA PVQSRLRSLS
     ISMGFPVDLA AVFLGGPWVA ALVATIGSGT QLVSLRWYKR LFNAAQIGVS AFVAGLVYRQ
     LPGASVGFAD PRFPHVLPAV IVTGLVLAVL NYSFVATAIA LAERLPIGRI WWGGMSETLL
     PSMGYGFIGL AIAVVWASGV GVLAGVLVLA PMLAARWAFQ QYGAQHAAYE ATVASLIQAV
     ETKDYYTRGH SERVARAAVM IGRRLGMRED RLEMLRYAGM LHDVGKLGVP TRLLQKTGPL
     DAAEFSAIKL HSVRGCEVIG DIEFLGEAAK GIRHHHERMD GLGYPDGLAG DAIPEFARII
     AVADAFDSMT STRSYRAARS VEAAITELRR WSGTQFDPVM VEALIAALQE EGWTPAAPPA
     GVAPAALLFG DHDDPASQVA AVLQPVAERV S
//