GenomeNet

Database: UniProt
Entry: A0A1E7ZB07_9ALTE
LinkDB: A0A1E7ZB07_9ALTE
Original site: A0A1E7ZB07_9ALTE 
ID   A0A1E7ZB07_9ALTE        Unreviewed;       712 AA.
AC   A0A1E7ZB07;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BFC18_11845 {ECO:0000313|EMBL:OFC70703.1};
OS   Alteromonas confluentis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC70703.1, ECO:0000313|Proteomes:UP000175691};
RN   [1] {ECO:0000313|EMBL:OFC70703.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC70703.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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:OFC70703.1}.
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; MDHN01000025; OFC70703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7ZB07; -.
DR   STRING; 1656094.BFC18_11845; -.
DR   Proteomes; UP000175691; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR029095; NarX-like_N.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000175691};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        170..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          232..448
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          464..581
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          595..709
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         514
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         644
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   712 AA;  78979 MW;  26CC7472882C8645 CRC64;
     MLAACAITLL MTGYFVWTQS YLDATQIQPK IINIAGYQRM LSQRIAFLQT LLTDESKEVE
     QKRLRNELIA RTSEFLRNHE ILVGRQPLEG VFTPLSEELE QLYFSDEGAL DKKALQYGEN
     ALYLASASAA RGSNLKPVTL AAATAMLRNL DRAVQLFEMQ LSRDIKFNQM MLLAVWFITT
     CLALLIILLL FRPLKNLVLA QFAMVQETRN DILNEREQTN RMMSSTEEFI KAMSREFRSP
     IAVIIGALEL LPNAKNRQAA LLQKAENACY TLLSLSSNLM ESLSGDTSVT AKAEDFILVR
     ALDDAYSEFL YNCQKKNLNH QIVNDSSLPY LVHGYPELLV KALKSVLDNA IKFTPHGMVS
     VYNRMAIVDG ARVIIIRVVD TGIGIHEDEL ERIFERFTTS YDPAYSFSGA GTGLYTARKL
     LAKAGGSITV SSALQSGSEF TLTVPLESAK HQPEALTNDQ FSNRFAVVDD QEITRIYIQS
     MIEAEGFAVD TYKSGADLLA NQEKVKSYSG IITDYFMPGI NGVELITYLQ AIMGKNMPPV
     MMVSASPHIA NVIANSDATA WQVFVKPIDK NRFTDAIKAL ASNKSLHAPP SGDFSVLVVE
     DESINAEILC DMLENMGYDV SIAADGETAL HKAIEKNYDA ILLDLHLPDI SGFEVATLLK
     ERGCQSKLVS VTASAYPADA QRAFAAGIRY HLVKPVAYQE LKSMLRLLLV QD
//
DBGET integrated database retrieval system