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Database: UniProt
Entry: A0A385C8V3_9GAMM
LinkDB: A0A385C8V3_9GAMM
Original site: A0A385C8V3_9GAMM 
ID   A0A385C8V3_9GAMM        Unreviewed;       935 AA.
AC   A0A385C8V3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BEN71_16025 {ECO:0000313|EMBL:AXQ23483.1}, CDG68_18885
GN   {ECO:0000313|EMBL:AYO55585.1};
OS   Acinetobacter wuhouensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ23483.1, ECO:0000313|Proteomes:UP000257257};
RN   [1] {ECO:0000313|EMBL:AXQ23483.1, ECO:0000313|Proteomes:UP000257257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ23483.1,
RC   ECO:0000313|Proteomes:UP000257257};
RX   PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA   Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA   Nemec A., Zong Z.;
RT   "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL   Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
RN   [2] {ECO:0000313|EMBL:AYO55585.1, ECO:0000313|Proteomes:UP000279962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHAW010062 {ECO:0000313|EMBL:AYO55585.1,
RC   ECO:0000313|Proteomes:UP000279962};
RA   Hu Y., Long H., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter wuhouensis strain WCHAW010062.";
RL   Submitted (OCT-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   -!- 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}.
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DR   EMBL; CP031716; AXQ23483.1; -; Genomic_DNA.
DR   EMBL; CP033133; AYO55585.1; -; Genomic_DNA.
DR   RefSeq; WP_068973280.1; NZ_SGSR01000024.1.
DR   AlphaFoldDB; A0A385C8V3; -.
DR   STRING; 1879050.GCA_001696605_00572; -.
DR   KEGG; awu:BEN71_16025; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000257257; Chromosome.
DR   Proteomes; UP000279962; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C: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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
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   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; 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; 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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000313|EMBL:AXQ23483.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AXQ23483.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          296..523
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          666..791
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          829..929
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         721
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         868
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   935 AA;  106579 MW;  BEA4349FF645C0DC CRC64;
     MSNFNKKLFK RLKLNHAYGQ LIALIFVPIM VLACVGTALV LSETSSAAKS KQRFQAIAIL
     SRYQYTAEKL TAVMEINKTQ HIKAENILQK MFNEKHLLSA AVIDANNINH LSIGYQSKRT
     WPQIPKSGTF FGPIQSKTNN IYGIKLNPIN STENMWLVIE MDNQPLEIAH YRVMIVLITT
     ALFTLLLLLL CLNFYSRRWI APMYEIRMQL QRLNADTLDQ HMVINSTGEL RLLQRDIANV
     VKRLHFSFLE LKEHTEQTED DLRRTLDTLE VQNITYKQAR DQAILSNQSK SVFLANISHE
     LRTPLNSIDG FIHLMLRQDN LSNDQSLYLQ TIRKSSAHLL ALINDVLDFS KIDAGKLELE
     TAPFDLEEAI FDVMDMLSPL AAQKHIEMAF YFADNVPKYV IGDALRFKQI LTNLISNAIK
     FTPDGEIIVR ARMEHDDIGQ CLLHFSVQDS GIGLSGTDRK KLFESFSQGD ASVTRQFGGT
     GLGLAISKQL VHLMHGQIGF EDNQERAPTE KGSTFWFTAM LAVNEDEDIV HPSFSEQKVV
     SYLAHPATAN VLRHYLEDYQ VQHNEAQSIL DLFSRLNSLG QDTDNTWLIV DHSGDTEALL
     KEIRGRYQGH LAVYGYQMSL DPNMLSEYKA RPLYQPLSRS SVIQLLSNKP VFEQEQHKDF
     KGQDLHILAV DDHLPNLIVL EALLGELNVK TTKAQSGQEA LTIIQQGIEQ GSKPYDLVFM
     DIQMPVMSGI DTTRAIRSLE STLDGMRMPI IALTAHALAD EKQKLLKVGM DDYVTKPIQI
     EQIIQILTNW TSDKFIQQKQ QTNENKVYIE AFNTDILDWK QSLALAANKE DLAQDLLKML
     VDSFPTELDE IEQLIELEDF PQLEHVLHRL YGATRYVGTP KLQRVTGEFE QFISTLRKER
     RKADENFIQE VLRRLDDLQV AIREVETAAQ QILPN
//
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