ID A0A434AX82_9BACT Unreviewed; 1190 AA.
AC A0A434AX82;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DLK05_06040 {ECO:0000313|EMBL:RUT79036.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT79036.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT79036.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT79036.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RUT79036.1}.
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DR EMBL; RJJX01000005; RUT79036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AX82; -.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000282985; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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; 3.30.450.20; PAS domain; 6.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 6.
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; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 6.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:RUT79036.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000282985};
KW Transferase {ECO:0000313|EMBL:RUT79036.1}.
FT DOMAIN 189..233
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 331..384
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 390..442
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 443..513
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 515..567
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 568..626
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 687..733
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 760..812
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 830..1048
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1072..1187
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 19..46
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1122
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1190 AA; 137626 MW; 2419427F6CD11BA6 CRC64;
MQCNKKNLLQ ESNFKNRIMA EQDKTKGELT KEIKRLQQEI GSLKASFDNS VVRDKQELKK
QILSKSELQV LIDNKKESIW SIDNNYNILA CNNYFKNAFF AAYQQELKVG MNILETLSPE
LLAFWKPKYD AALLGKNISF EFSETILGEH YYFNVDLNSI LENGEIKGVA AFSVDVTTLK
KTEESIIKSK KLHRNFLENN EAVILAFETE TSRITFANNS AVEFYGWEKE QLLQMNINQI
NTLPPKEIKS KIIEARKKNH NFCTFKHRLA NGSIRDVEVY QTKLNLNNKE IFSLIVHDIS
EQKKVEEALR WAKFKFRTFA DYTADWEYWE NEDNKIMYMS PSCEKFTGYT ADEFISNPEL
ANSIIHPDDL NAVLKHHDKT YSYHDRDKLE NIEFRIVKKD GFIVNTYHTC RPIYDENKDF
LGRRVSNRDI TERLQSRKAL QESEKRFQIL FNKAPLGYQS LDYKGNFIEI NQQWLDMLGY
SREEVIGNWF GKFMTVSSQE KVKNTFPLFL KQGYINTKFE MVHKNGSLLT INFVGKIGND
SNDNFLQTHC ILQDITASKI AEDALKESER KFRRLFDDHA AVKLLIDPET GNIADANKSA
IAFYGWSYEE LKSMNIDQIN TLEPEELRRE MGDARNNSRN FFEFRHYLKN GKIKDVAVFS
SKIEIEGKEY LHSIIQDITQ SKLAEKQLKL LGQAIDQNPV IILIANKVGE IEYVNPIFTK
VTGYTREEVM GKNPRFLQSG EHKHEFYKEL WDTITSGKNW HGEFHNKNKN GEYYWENAII
SPVFDDHNKI LHFLAVKEDI TEKKKMISDL IAAKDKAEES DRLKSAFLAN MSHEIRTPMN
AILGFSELLK EPDLANEQQQ DYIALIEKGG ARMLNIINQI MDISKIESNL MEVSIKEINI
NKQIEHTYNF LRSQVEAKGL EISYKTPLQD KDAIIKTDPD KVLAVLLNLV NNAFKYTDKG
TIEFGYEKKD KYLEFFVKDT GIGVPQNRQK AIFERFIQAD IEDKMARQGA GLGLSISKAY
VEMLGGKIWL VSEKDRGSVF YFTLPYNTDK AKNVILKNVI SASGENYAKN LKILIAEDDE
TSEKLAEIMI DKFGKEILIA RTGQEAVEIC KNNPDIDLVL MDILMPEMNG LEATEKIRQF
NKEIIIIAQT AYAMKGDREK AINAGCNDYI SKPIKKSILL ELMKKYFKKD
//
