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Database: UniProt
Entry: L0W9U1_9GAMM
LinkDB: L0W9U1_9GAMM
Original site: L0W9U1_9GAMM 
ID   L0W9U1_9GAMM            Unreviewed;      1048 AA.
AC   L0W9U1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:EKF73513.1};
GN   ORFNames=A11A3_13285 {ECO:0000313|EMBL:EKF73513.1};
OS   Alcanivorax hongdengensis A-11-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF73513.1, ECO:0000313|Proteomes:UP000010164};
RN   [1] {ECO:0000313|EMBL:EKF73513.1, ECO:0000313|Proteomes:UP000010164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-11-3 {ECO:0000313|EMBL:EKF73513.1,
RC   ECO:0000313|Proteomes:UP000010164};
RX   PubMed=23209226; DOI=10.1128/JB.01849-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT   hongdengensis Type Strain A-11-3.";
RL   J. Bacteriol. 194:6972-6972(2012).
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:EKF73513.1}.
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DR   EMBL; AMRJ01000024; EKF73513.1; -; Genomic_DNA.
DR   RefSeq; WP_008929827.1; NZ_AMRJ01000024.1.
DR   AlphaFoldDB; L0W9U1; -.
DR   STRING; 1177179.A11A3_13285; -.
DR   PATRIC; fig|1177179.3.peg.2639; -.
DR   eggNOG; COG0834; Bacteria.
DR   eggNOG; COG2206; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   OrthoDB; 9764808at2; -.
DR   Proteomes; UP000010164; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00077; HDc; 2.
DR   CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR43155:SF2; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108; 1.
DR   PANTHER; PTHR43155; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108-RELATED; 1.
DR   Pfam; PF13487; HD_5; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 2.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:EKF73513.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        578..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          601..654
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          825..1028
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000259|PROSITE:PS51832"
FT   COILED          39..66
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1048 AA;  118163 MW;  5CF0B76FCEC28BA9 CRC64;
     MARKQWTYSI RLGVVSIFVF ATVLTACVAI GLQYYFNYQQ ALETAKAQYQ ATAEQAASEL
     EKLDLRASDV ARTLTRQLPL ITDTGQINRN TARWFADVLA LNPAFYALYI GHDNGDFFEL
     INLEADPQAR ERLKAHADER WVIMSIRQRQ DARQQSYRYL NDKLVTLRQR DVFAAYDPRT
     RPWYRGANSK RVFKTPVYLF NNNLSGKTYS LRLPGGDAVL GLDVALSSFT RTLVNMPVAN
     GTELYLYDNN GALLASNQPR HQAGPLPSVT PLTLSDDEQA LVSKLGPLRV SNELDWPPLD
     FAIAGQPSGY TIDTLKLISQ MTGLQFRFIN GENWTGLMAL FQQGKIDLLQ PVLPSRDNRQ
     RGQLTEPLIQ LPFALASRAD QDPYTSLSQL QGKTLAVGEN WSIIPAIRDS YPTIKLREYA
     STLDAMKAVV RGDADAVVDN TIVLQYCRHQ FFLQALQISQ SDTIGLPDSQ GSLSLMVHDD
     QPALLALLNR AIARIPADAR QQLAQKWLLD PQSLNRLTAT LPYPPLLNPD TREGNLGQFN
     QDDVQHFFYT RSLGERGAMN FAAVISQPMI TGAAADNALL AAGITALCMI ILLPFAWLFA
     NPIVRPIKQL EAQSHHVRER RYDRVSRVPT RITETEKLAD SLYQMAQAIG QHEKQLEALM
     EAFIELIAEA IDGKSPYTGT HCARVPILGM MLGDAASLSS DGPFRDFSLD DDKKRREFRI
     AAWLHDCGKI TTPEHIVDKG AKLETIYNRI HEIRTRFEVL WRDAQIDYLT ACQANPHQQD
     ELRQRWQQRQ QQLQEDFAFI AAANQGSETM SEADKNRVRE IGAHTWQRHF DDRLGLSPLQ
     SRQLGPSTTE LPVTETLLQD KPEHLLAHEH TTEYDPRLGI RMQAPEWRAN LGEVYNLTIE
     RGTLTPEDRF KINEHIINTI RMLDSLPFPE DLAKVPQYAS THHERLDGKG YPRQLTAEQL
     EIPDRILAVA DVFEALTAAD RPYKDAKTLS ESLAIMKAMV ADGHIDGQVF ALFLRSGVCL
     RYAQHYLSES QIDVQDLDAY LPSSPGYS
//
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