ID D5VMC7_CAUST Unreviewed; 1128 AA.
AC D5VMC7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cseg_3213 {ECO:0000313|EMBL:ADG11650.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG11650.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- FUNCTION: Essential protein that is involved in the control of cell
CC division, probably through the regulation of ctrA. Its phosphorylation
CC status is regulated by PdhS. {ECO:0000256|ARBA:ARBA00037447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBUNIT: Interacts with DivL, PleC, DivJ and PdhS.
CC {ECO:0000256|ARBA:ARBA00038776}.
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DR EMBL; CP002008; ADG11650.1; -; Genomic_DNA.
DR AlphaFoldDB; D5VMC7; -.
DR STRING; 509190.Cseg_3213; -.
DR KEGG; cse:Cseg_3213; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_000445_127_0_5; -.
DR Proteomes; UP000002629; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADG11650.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 467..687
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 736..849
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 858..975
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1004..1126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 377..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 785
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 907
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1059
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1128 AA; 123927 MW; 2250A482B1AAA873 CRC64;
MEVWAAFGLA LVLLFFLASG MVAYRNVTVL RANSQQIWHS HDVLMAIDDL LSTVQDTETG
QRGYLLTGND RYLEPYQEAA SAVVSRTDAV RNLTRDNPTQ QANLAVLERR IASKLIELEE
TIALRRTQGA QAALAVVNTD RGKSEMDAIR QQIGVMRQEE NRLRDIRLSQ MGAAYDTALL
SGVLASVLGA ILTLVVFYLI RRAARAQARG EWLQAGQVGL SSAMMGDLSV EMLADNILDF
LSKYVGFQAG VLFKGHGGHF YRAASLGIPA DAQTPERFNL KEGLLGKVAA EGKATIIRDV
PDGYISVGSA LGHDKPKHLV IVPVKADGVV NAVIELGFLH PVDDRVLTLL EQASSTIGVG
LRSARYRAQL QDSLEETQRQ SEELQVQSEE LRVSNEELEE QGRALKETQT RLEQQQAELE
QTNSQLEEQA QMLETQRDDL ERTSAAVALK ARELEQASQY KSDFLANMSH ELRTPLNSLL
ILSKLLSDNP NGNLTAEQVK FAQTIESSGN DLLSLINDIL DLSKIEAGHI EVRPESVSLQ
RLTGDLRQLF NPVADSRKLD FAIEVAADCP LVVETDRQRL EQVLKNLLSN AFKFTEKGGV
RLEIKAASND RIAFAVKDTG IGVSRDQQEA IFEAFRQADG TISRKYGGTG LGLSISRQLS
RLLGGSITLE SQPGEGSVFT VTIPVAYDPA RVAPREPPRL AETPVAAPAP RPHAKRTTPP
KTVEDDREQA AGARRVLLVV EDDDTFASIV RDMSREQGFQ CLVANTAEEA VKLAREFKPS
AVVLDVGLPD ESGLLVLDRL KRDDATRHIP IHVISAEDHS QTALSLGAIG YLVKPVKRDD
LTEVLKTLEA KLASTVRRVL IVEDDPVQRE AVGKLLTSGD VETVGVGTAA ECLEALKRET
FDCMVLDLSL PDASGYSLLE TLSQNGDHAF PPVIVYTGRD LSADDEQRLR RYSSSIIIKG
AKSPERLLDE VSLFLHQVVS ALPPEQQKMI QKARNRDAVL EGRRILVVED DIRNVYSLTN
VLEPRGAVVE IARNGQEAID ALGRAAQDPS EEIDLVLMDV MMPVMDGLTA TRAIRNDPRW
SKLPILMLTA KAMPDDQARC IEAGANDYMA KPIDVDKLLS LVRVWMPR
//
