ID A0A2S6NJY3_RHOGL Unreviewed; 1264 AA.
AC A0A2S6NJY3;
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=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CCS01_08420 {ECO:0000313|EMBL:PPQ35217.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ35217.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ35217.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ35217.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:PPQ35217.1}.
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DR EMBL; NHRY01000076; PPQ35217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NJY3; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
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; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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 Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000239724}.
FT DOMAIN 196..268
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 272..324
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 403..453
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 479..552
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 554..607
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 625..849
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1005..1122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1158..1255
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 444..489
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1054
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1197
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1264 AA; 137118 MW; 5D561115D699C444 CRC64;
MFDAPPQELT RLVHVLHETQ QRIQALTGGS VDAVLDADSG ATYLLPASQA HLRHSEHEQR
RFATERASIL NALPAHIALL DAQGHIVVVN ETWRCFAIAN SYPSPEFGAG ENYLDVCDRA
TGDCAAEAAA VAAGIRAVIG RKAPRFDNEY PCHAPDEQRW FHLIVTPLGN GDAEGAVVMH
IDITRRKLAE QALRASEERF RLLSNATNDA ILDWDRNAGT MWWSDSFETL TGLSREHDSP
TTDAWRHRIH PDDRAGIVAG IHRAMDGDAT SWSAEYRFLR WDGEYAYVLH RVQVIRDAFG
KPVRLIGGMT DLTERRRTEQ RVAEQTALLA AEAEKHRTLF DRAADGIAVV TDDGCLIDAN
SRLMAMLRAS GSEVLGSHVW DWDVNFDDQV AWRRLRASMA HSPLVQTRIR RRDGTLFDAE
VMNRVADLPG GRLLYCSMRD VSDRKKAEQE LALYRTHLER LVRERTSALE EANRRLRVSE
ERYAHAAEAS SDGIWDWDVT TGAITFSPSW LSMLGYMPEG FVPHVDAWLA LLHPEDRDAI
VRDNLRRFAT NGTCEAEFRV RSRDGSYRWI LSRAKVVERD AAGMPARIVG THSDLTSRKL
AEAQLREARD AAEAANRAKS SFLAMMSHEI RTPLNGVIGM AEVLALDHLQ PRQAEAVGII
RDSAINLMML IDDILDFSKI EAARLDLDRA PVALAELVED VCNSLAPIAL DKRVDLSAVI
APECPRWLLA DPTRLRQVLF NVAGNAIKFS AGRPAIQGRV TIRVDVAQAT PLRIRICVVD
NGIGMSAETQ GRLFTPFTQA ETSTTRRYGG TGLGLAITRR LIDLMQGGIA VASAPGAGST
FTITLPFEIA DRPVAAMPDL SGIDCVLAWS ADSPDAADMK RYLSAGGAYV HAAADPAAAM
ALARTLGGTV VVIHDAGRTR NDAAAPAHVH WLLLRRAQRW RAWLDPGDET GLDLGWMRHE
ALLRAVAAAA GRLPRSALAA AKPIGALLPA APPPTVAEAR AQGRLILLAE DDEINRTVIL
RQLNLLGYAA ETASNGREAL EKWRGGHYAL VLTDVSMPDM DGYQLTTAIR QEEAGARRTP
VVILSANALR GEAERARAIG IDAYLTKPTL LRDLHAALQD VLSGAPSPQA ATGGDVAAPA
AAPAAFDSHT LAAIVGDDPD VIAAILADYS RSAERLAGEL AQAAADGDAA RVGAVAHRLK
SSSRAVGALL LGEICAVLEQ AGNAGDLNAV PACLPTFSAA MAAVQERIGD QLEHRPRGAT
SGTS
//
