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Database: UniProt
Entry: U1L052_9GAMM
LinkDB: U1L052_9GAMM
Original site: U1L052_9GAMM 
ID   U1L052_9GAMM            Unreviewed;       903 AA.
AC   U1L052;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PMAN_14429 {ECO:0000313|EMBL:ERG25330.1};
OS   Pseudoalteromonas marina DSM 17587.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG25330.1, ECO:0000313|Proteomes:UP000016528};
RN   [1] {ECO:0000313|EMBL:ERG25330.1, ECO:0000313|Proteomes:UP000016528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(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   -!- 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:ERG25330.1}.
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DR   EMBL; AHCB02000044; ERG25330.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1L052; -.
DR   Proteomes; UP000016528; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; IPR007895; MASE1.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          261..466
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          541..762
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          782..898
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         831
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   903 AA;  100702 MW;  C22BEAFA4B4E5630 CRC64;
     MKIFASTSQS IIFYILFALA YYLLGVGLTA FAFNSQIVPI WLPAGIALVG CYIWWWRFIP
     PLFAAAIAFN LNIFDNSAHE IMLVGNTFTQ AIYIALGVII QAMVGAAILR YWLGNPLYFR
     KRKYIAYFIA VVAVLVSLLS SNIGVFALSN FNPLYSIEDH WLHVIYWWLG DILGVLIASP
     FLLSLLPKAP GQRKVLAFET IAVCSILFIS VALTAQIYER ENSKNTIKIA EREVEVIENS
     LYRYINQSII AVQSLASQVQ SSPEFNEQDF YASANKLLEK HSFIKALSWN VQITQAQRQT
     LSNTMSTIYR QNINIVGDPL EDDDPLVVVK YIAPLESNQK AVGFNVYSNP DRKASLQNPA
     IKYLPISTKI IQLVQTKTPT PAYLLFAPVY GQNENIKGYA TGVFLAHKII EQAITQQQSE
     MFSIDVFEFD NEPAFYSNDS QNFEQATQSQ LMSFNINFGG QQWVIKLALK ENYISQQNIE
     MSLFLLMLQT AVCLLIIVVL MLFNQQQLAL SRQVAERTSS LVKAKKQSDL ANSAKSQFLA
     NMSHEIRTPL NAIIGLSSLA KKGDDAQKLF SYIKKIYSSS NSLLNLINDV LDISKIESQH
     LILESIAFDP KALVTRIDTM FEQSAKNKNI EWILKCNLPV DTWFLGDAMR IEQILLNLCS
     NAIKFTNEGS VTLDIDTEFV SANKVKLSIS VSDTGIGIEK NQHNTLFNAF TQADSSTSRK
     FGGTGLGLTI AKELCLLMGA TLNLKSELGE GSTFTFAVNL TTSEPDIEPE AISKDIDITS
     LNILVAEDNP VNQMVIKAML GSLGIIPHLV ENGEEAVNII KEQHFDLVLM DCQMPVMDGY
     KATELIRAFK SQHTLPIIAL TADAMPEDKI KAKKAGFNEH LAKPIELAKL TECLSQFVKT
     VTK
//
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