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Database: UniProt
Entry: K4L1K5_SIMAS
LinkDB: K4L1K5_SIMAS
Original site: K4L1K5_SIMAS 
ID   K4L1K5_SIMAS            Unreviewed;       355 AA.
AC   K4L1K5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Response regulator receiver modulated metal dependent phosphohydrolase {ECO:0000313|EMBL:AFV00058.1};
GN   OrderedLocusNames=M5M_14605 {ECO:0000313|EMBL:AFV00058.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00058.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFV00058.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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DR   EMBL; CP003746; AFV00058.1; -; Genomic_DNA.
DR   RefSeq; WP_015048210.1; NZ_ATUQ01000009.1.
DR   AlphaFoldDB; K4L1K5; -.
DR   STRING; 1117647.M5M_14605; -.
DR   KEGG; saga:M5M_14605; -.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_000445_92_10_6; -.
DR   OrthoDB; 9787688at2; -.
DR   Proteomes; UP000000466; Chromosome.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd17551; REC_RpfG-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45228:SF1; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186; 1.
DR   PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR   Pfam; PF13487; HD_5; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AFV00058.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466}.
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          151..348
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000259|PROSITE:PS51832"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   355 AA;  40180 MW;  3C9076DDF02B6453 CRC64;
     MKVHQGKVLI VDDNAVNIVI VEKILRQDGF NNIYSTTDAK SVRDLYREHD FDAILLDVHM
     PEMNGFDVMA ELQADNPDDY LPILMLTADH TPETRHLSLS SGAKDFISKP FERVEVLFRV
     RNIVEVRMLH KEVLNANEVL EDKVRERTQQ LYEAQIKLIE CLGKAAEYRD NETGMHVVRM
     SQSSALLARQ MGLSAEECEI ILHASPMHDI GKIAIPDSVL LKPGKLEGKE WRTMQSHAEV
     GAQILASYDS KLMEVASIIA RTHHERWDGK GYPEGLQGEE IPLYTRIVSV CDVFDALTST
     RPYKVAWPVS KALGYLKENS GSQFDPQVVN EFIAIIDQVL EIRQQYPDSQ SAGQH
//
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