PLH4_FORAG
ID PLH4_FORAG Reviewed; 1370 AA.
AC T2KMF4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Histidine kinase P4 {ECO:0000303|PubMed:31285597};
DE Short=P4_HK {ECO:0000303|PubMed:31285597};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q8KIY1};
DE AltName: Full=Polysaccharide utilization locus H protein P4 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P4;
DE Flags: Precursor;
GN ORFNames=BN863_21930;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: Histidine kinase probably involved in ulvan degradation
CC (Probable). Ulvan is the main polysaccharide component of the Ulvales
CC (green seaweed) cell wall. It is composed of disaccharide building
CC blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic
CC acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
CC {ECO:0000305|PubMed:31285597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q8KIY1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:31285597}.
CC -!- PTM: Autophosphorylated. Activation requires a sequential transfer of a
CC phosphate group from a His in the primary transmitter domain, to an Asp
CC in the receiver domain and to a His in the secondary transmitter
CC domain. {ECO:0000305}.
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DR EMBL; HG315671; CDF79905.1; -; Genomic_DNA.
DR RefSeq; WP_038530482.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KMF4; -.
DR SMR; T2KMF4; -.
DR STRING; 1347342.BN863_21930; -.
DR EnsemblBacteria; CDF79905; CDF79905; BN863_21930.
DR PATRIC; fig|1347342.6.peg.2200; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OMA; LWFATEE; -.
DR OrthoDB; 1635706at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW DNA-binding; Kinase; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transcription; Transcription regulation; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1370
FT /note="Histidine kinase P4"
FT /id="PRO_0000448297"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 852..1072
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1119..1234
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1266..1365
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 1284..1305
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 1332..1355
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT MOD_RES 855
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1167
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1370 AA; 156432 MW; 63E22E4A22E57146 CRC64;
MRNIGVFSVI LFSFLAISLK AQNSNFVFKS FTPIDGLSQS SVIDIEQDKI GQLWVGTRDG
LNKFDGHTFK IYRNNPEDST SISNSDILSI AEDRSGMLWV GTYNGLNKYN PETNRFQRYF
HSNESTSLPS NTIWKLKEIK NEIWIGTLNG LAIYNKKTEG FTSVLSDEKN KSSLPGLFVT
SIFESTNGDI WVGTDNGLCK LISRNAEQIS FQTINYKKNK DIRPYKLHVK DIIEDKNHNL
WVATKNSGLY MIKANTTTLI SYQNTPDFKD VNLDIRAINF DKHNNLWIGT YSGIFILKSD
GDVQHIGKKS SDYSGLNKIK TIFTDKHGSV WAGSYYGGLH LWDESNSNFI NFNQNSKSLR
LSYNVVGSIA ASKDSLVFFG TEGGGITQYN FKSDESIYIN SENTKGFLSD NIKSLKIVDD
ALWVGSFNTL PFLYDYNTKT VRTNNFPDEL KNIFIESSVY FTEKENDSII WFGTFGSGAI
RYNTETKNYI QLTTEPEGLY SLTNNRVRTL FIDSKQRVWL GTQSGLNVMA LSNIDKEKIP
IKQFFFDSEL ISGVDILTVF EDSNRNIWVG TKASGFYVYK GETFEKVDIQ HNGVKVNSVH
SVLEDAYKNL WLSSNQGLVK YNLNTKNITI YDQTDGLISN EYNDNSSLNF NNDTFYFGGP
AGVVSFQPDQ ISLNNYNPQV ILTDFRIKNE SVPIGGDQAI LTKDIAFTKA IDLDYNNANF
SIRFAIPNFI NGSNNQYAYR MLGLEEAWNV TSNTEANYII QQAGNYTFEV KGANNDDVWN
EQPTILNITV HPAPWRSWWA FCLYALCIGT ALIALISFLK SKAKLKHKLA LESIEKQRNE
EINQAKLQFF TNISHEFRTP LTLILGPLQQ VLLDYKGSNK VYKKLLVIEN SANHLLQLIN
RLMDFRKLEN SQFNLQAAEG NIVKFLKEIY FSFSEYAKNG NYTYTFESES DVINVYYDRS
KLERVFYNLI SNAFRYTPEG GNITLKITTD SKYIYIDIND SGVGISDEFK TKIFNRFFEV
PIHNQPQKNY NKGSGIGLSI AKNIAELHKG TIRLVHKERP GTIFRVSLPL GRGHLQDSEI
ISDFKLSDDI SQYEIQLETL PVLDEDSIED LITEKEKSTI LIVEDHKPLR VFIKNLLKHD
YNILEAENGK IALKLAQQNL PSLIISDVIM PEMVGTELCS KIKEDIKTSH IPVVLLTSRS
SLIYKFEGLE SGADEYISKP FNVKEFRLRI KNILENRMRL KAKFSNAKHI TPSEITISSI
DEQLLKKAFK IVEDNMANEQ FDVLAFSQEL GVSRTTLFNK IKAWTNFTPN EFIQEIRLKR
AAQLLETNKI NISQISYQVG FKSPKYFSKC FQKKFNETPS QYQNRYSEQF
