ID A0A2T6AU49_9RHOB Unreviewed; 911 AA.
AC A0A2T6AU49;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C8N34_113100 {ECO:0000313|EMBL:PTX47344.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX47344.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX47344.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX47344.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTX47344.1}.
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DR EMBL; QBKP01000013; PTX47344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6AU49; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000244224; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR038188; TorS_sensor_sf.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PTX47344.1};
KW Membrane {ECO:0000256|SAM:Phobius};
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 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..391
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 434..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 675..787
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 372..424
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 724
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 911 AA; 97175 MW; E34B07C13382E9CB CRC64;
MVLFGLMVVV GLASFGVNRF LAQTQQRVLS ESIAIIERTE RVAQDADFAA ALAGQLAAAR
ELRQSEDLAR ALQLRIDRIA ADLEVTRAFL GRAPEPDSAT PVRGVVTEME STVAVLIEAT
ELELTERASL SEAGAMLSAL ISTEADLARL RVTAGIWELY SLPSGADTRP ELDRLADANF
FAYERLAEMA EAVSTFGQLL ARVGMAGRNA ELDALERDYQ AEVALMQDRV TFMLSARSRA
MASDIVAELA QGLTVDGVIA QRRSALQAKE ALDALSLELG RQLDLLIAEA LQGRVETRER
MQTAVAASGW QATLLSAALA GVILLALFAG YMVWTRIRRR VVLRLEGVAD RMVAMADGDL
GQALTISGAD EIGRLEAALN ILRDRAEEAM TLRGRLEAAV LDRTAEVVAE MQSANAARAD
AEEQSRAKTH FMARMSHEIR TPLNGLIGLL DLLGADEADA GRRARLEVAL TSARDLQELT
EEILTFSVGE DGQDQKRLAA FDPTVVAQGL AAHLDVIAAA KGLQAVVRID PDLPPALVGE
PTKIRQVMMN LLSNAVKYTA RGSVTLSVGA RPIPPGKQEL SLCVRDTGPG MTADETRQAF
DIYGRSRSAR QSGVKGVGLG LAIVRQLTDA MGAELRISTL PGRGSSFTLV LSLPEADPDA
ISALPPEPAA GAGRRVLVVD DHPVNRLVAR GYLERMGCRV TEAATGQAAL AAARDGDFDA
MLVDLNLPDL SGDAVVSQIV RKGARVAVLT ADLVRDDAET RERFGVDRVL TKPISPRALA
SFLEGGEPLP AAETAPGSVV DVALRDDIAG LGAEQTAEIV AALMADILAA VPLLRDFPDP
ETRRKLAHRL KGAASNFRLE PFCNLMQRIE AGEPSALETL NSVASNAINE LASAARRAGL
DLQPFAKPAK T
//
