ID A0A1M4XM96_9RHOB Unreviewed; 1148 AA.
AC A0A1M4XM96;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444339_102535 {ECO:0000313|EMBL:SHE94704.1};
OS Loktanella atrilutea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=366533 {ECO:0000313|EMBL:SHE94704.1, ECO:0000313|Proteomes:UP000183987};
RN [1] {ECO:0000313|Proteomes:UP000183987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29326 {ECO:0000313|Proteomes:UP000183987};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQUE01000002; SHE94704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4XM96; -.
DR STRING; 366533.SAMN05444339_102535; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000183987; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHE94704.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000183987};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..702
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 756..869
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 878..994
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1024..1146
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 717..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..475
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 805
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 927
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1079
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1148 AA; 125604 MW; F3FE1320B19AA331 CRC64;
MHRKQDIAGK FGWLGFGPMT TLGLVAALSF FVLSGAISIY VTARLQGSND RVVQTHQTIV
AVDQLLLDVQ NAETGHRGFL LTGDEQYLAP YLAAVGRLAS RLSQARALVV DDGAQRAQFD
ELEITIQDKF DIMEQSITTY RTAGQAAAIA EMNADEGIAV MDTIRSLIAD LRSAETDVRT
QRLDRMARDF RFADFVSIAT GLLGAALTVI IGLIMRRAAL AARRQQWVQT TQLGLGEHVA
GELSIEQVAQ RTLQALTNSL GAVAGTLYVE KDDNFDLAAV QGVPDKSAIA ARLGKSDSLF
SHVLQDHRPI AVGEVPEGYM AFGSGLGQAR PRYLALAPAI VDGEVAGLVE LGFLNPIPEQ
VLTLLERASS TVAVAIRSAA YRTRLRELVL EMQQQSETLQ LQGEELRVSN EELEEQGRAL
KESAARLEVQ QVELEQTNSQ LEEQAEELER QRNHLEKANA DIQAKAREVE QASRYKSDFL
ANMSHELRTP LNSSLILSKL LADNADDNLT PEQVKFAQTI HSAGNDLLDL INDILDLSKI
EAGHVEINPE PVSVQRMVDG VRRLFDPLAK DKGLDFVVNV ADDVPAEIRT DPQRVEQVLK
NLLSNAIKFT QGGRVTLKVR QTEDDRIALA VTDTGIGIPD DQQRRIFEAF HQADSTISRR
FGGTGLGLSI SRELVRLLGG TLQLTSKPGE GSTFTVTIPA AFDPEAVKPA LAAMAEPAVA
AQDDPAEEPP VPAKPRPATP QIVQDDRQAA ADQARTLLII EDDPAFATIL RDLARELEFR
TIVANTAQDA LDLARQQMPS AIVLDVGLPD QSGLSVLDRL KRDVRTRHIP IHIVSGEDAA
DRAMSLGAIG YAMKPVLRDE LISVLQSLDA KVSQATRRVL IVEDNAVQRD AVAALIASHD
VETVGAATGA ECLALLKEQT FDCMVLDLSL PDSSGLALLD TISRDDSHSF PPVIVYTGRV
LSAEEEQELR RYSRSIIIKG AKSPERLLDE VTLFLHQVVS DLPDEQQKMI RKAHNRDALL
EGRRILVVED DVRNIYALTN ILEPRGAVVE IARNGEEALE KLRRAGGGSD TAIDLVLMDV
MMPVMDGLTA TRQIRANGDW KKLPIIMLTA KAMPDDQRRC IEAGANDYMA KPLDVDKLLS
LVRVWMPR
//
