ID A0A0B4XP12_9GAMM Unreviewed; 1218 AA.
AC A0A0B4XP12;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=S7S_09045 {ECO:0000313|EMBL:AJD48223.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD48223.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD48223.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD48223.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004387; AJD48223.1; -; Genomic_DNA.
DR RefSeq; WP_008737696.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XP12; -.
DR STRING; 391936.S7S_09045; -.
DR KEGG; apac:S7S_09045; -.
DR HOGENOM; CLU_000445_127_0_6; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000006764; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 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; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 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; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 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; 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:AJD48223.1};
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:UP000006764};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..260
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 559..792
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 831..944
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 953..1069
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1099..1216
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 424..549
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 880
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1002
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1149
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1218 AA; 137227 MW; C4BEDDF271F91118 CRC64;
MNWFTNLSIR LKILSVAAMG ILAFLAYFVY GFYNNEANIR QISTIEQTDV PVLENINESN
LAYAAVREAF IQALNQENDE LFVEAHSLAW RYKEALSRIA DINPTVHDDV EALIELVDSY
LAEADALAQL TMSHTASPQA IESQRQRVLT LQSQYEARQR AFEQGRYEAF RNKLSVSRED
SRNMQYVGLG ISILTFVLLS LIAWRVTRSI TKGLRYAVVA ADDIAQGNWD ADIQVRSRDE
TGRLLYAIRR MRDALKTARD EDRRSERLKS QLAEFNDTMR GDMTLQQLGN NVLNYMVPAM
HAQVGAFYMF DDQSGTLRLN SSHAMERRKH LAGDFSLGEG LVGQCALEQK QILLSRVPED
YLSVTSATGS ATPRNVIVTP IVHEDELKGV IEVAAFREFD EDDLNFLQQA VRALAISVHT
AQSRVRLAQM LEQTRLQAQE LEQQKRELGQ VNADLEQQAM DLSASESRLQ QQQEELKAIN
EELEAQTQAL RASEESLQAQ QEELRVTNEE LEAQARLMSE QKAEVTKKNR ELELLRQELE
EKVRELEMSS RYKSEFLSTM SHELRTPLNS ILILSNALSE NKRGNLDEKQ VEHASVIYSA
GTDLLSLIND ILDISKIEEG KMELVIDDIS PQELSEHFRR NFSHVAENRG LSFHVQVEDN
MPAHFFTDRQ RLEQVLKNML SNALKFTEQG SVTLKLDVPA EDERLPSRHL VKGETMRFSV
IDTGIGIAPD KQQLIFEAFQ QADGTTSRKY GGTGLGLTIS RELARLLGGE IAIHSDGEGQ
GSTFMLYLPI GSEDTVEVEA EPEQAPSPLG AMLAEIVQPL PEDGFLVREK SVLIIEDDTD
FANVLVDLAA DYGLEGHVCA DGESGLEYAR HYRPSAIILD IGLPGMDGWE VMERLKADPR
SKDIPVHFLS GKDERKKALD LGAIDFLTKP VNKDQILGAF AKIETAISKN VRRLLVVEDS
EIQHEGIREL FDQKGVEITA ATNGTDALQA LRNQVFDCMI LDLTLPDMSG FELLETIHNS
ADYDSVPVII YTGKDLTREE EAQLRKYADR IILKTERSSE RLLNEASLFL HWLESTLPGH
SRNAAQAVEH RDDVFEDKRL LLVDDDMRNI YALSAQLEEL GFDITIANNG REALEALDEA
PDMDIVLMDI MMPEMDGYQA MGEIRKQDRF GRLPILALTA KAMKDDRAKC IDAGANDYCS
KPIDMAKLTS LMRVWLHK
//