ID B8FJS6_DESAL Unreviewed; 505 AA.
AC B8FJS6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Response regulator receiver modulated metal dependent phosphohydrolase {ECO:0000313|EMBL:ACL02354.1};
GN OrderedLocusNames=Dalk_0649 {ECO:0000313|EMBL:ACL02354.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL02354.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL02354.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL02354.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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DR EMBL; CP001322; ACL02354.1; -; Genomic_DNA.
DR AlphaFoldDB; B8FJS6; -.
DR KEGG; dal:Dalk_0649; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG2206; Bacteria.
DR HOGENOM; CLU_000445_92_10_7; -.
DR Proteomes; UP000000739; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR PANTHER; PTHR45228:SF4; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF13185; GAF_2; 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; SSF55781; GAF domain-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 313..505
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 505 AA; 55945 MW; BC24A2221951BCB3 CRC64;
MSMHDYLKIL AVDDDPGVLN VFKTYFEHSD QYSIVTASDG PSALDVFSKE QPDFLFTDLA
MPGMDGIALS KRILEMDNTI PIVVMTAYPS MESTIMALQT GVSDFIVKPF KIRDVDFIIE
KVMAQKEIMV ENLLLKSQHA RKKELEKINM ELAATVEEME KLNFILRKVD WKKNSGELFD
QLTNISCEIS GGHLCYFQLL DDSTGSLYPL AHHAVTEELD NEDVPDFLDA LAKQSLDKAG
PAIWGKDPAS GLITPLHAAV SIPFNIKDKP LGAITVCKTG PGNGFSEQDL HYLSFLGKRA
ALVVENTALY ENLCQNLFST LYAFVEAIEA RDPYTKQHSA RVADISCIIG EHLGCSAREL
DLLDFSGKLH DIGKIGVRDK ILLKQAQLDE EEFRIIKTHP EIGANIVGHM GLLKEETQVI
LHHHERWDGQ GYPNKVGGED IPFLSRIMSV ADAFDALTSD RAYRKKVDDA AACEIIRKNA
GAQFDPVVAE AFLDLAAQGK VTSAL
//
