CCKA_BRUA2
ID CCKA_BRUA2 Reviewed; 945 AA.
AC P0DOA0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Sensor kinase CckA {ECO:0000303|PubMed:26124143};
DE Includes:
DE RecName: Full=Protein histidine kinase {ECO:0000303|PubMed:26124143};
DE EC=2.7.13.3 {ECO:0000269|PubMed:26124143};
DE Includes:
DE RecName: Full=Response regulator {ECO:0000305};
GN Name=cckA {ECO:0000303|PubMed:26124143};
GN OrderedLocusNames=BAB1_1059 {ECO:0000312|EMBL:AM040264};
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=2308;
RX PubMed=26124143; DOI=10.1073/pnas.1503118112;
RA Willett J.W., Herrou J., Briegel A., Rotskoff G., Crosson S.;
RT "Structural asymmetry in a conserved signaling system that regulates
RT division, replication, and virulence of an intracellular pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3709-E3718(2015).
CC -!- FUNCTION: Component of a regulatory phosphorelay system that controls
CC B.abortus cell growth, division, and intracellular survival inside
CC mammalian host cells. This signaling pathway is composed of CckA, ChpT,
CC CtrA and CpdR. CckA autophosphorylates in the presence of ATP on a
CC conserved His residue and transfers a phosphoryl group to a conserved
CC Asp residue on its C-terminal receiver domain. CckA-P transfers
CC phosphoryl groups to the ChpT phosphotransferase.
CC {ECO:0000269|PubMed:26124143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:26124143};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:26124143}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:26124143}; Cytoplasmic side
CC {ECO:0000305|PubMed:26124143}.
CC -!- DISRUPTION PHENOTYPE: This gene cannot be deleted or disrupted in the
CC absence of a complementary copy expressed in trans, indicating this
CC gene is essential in B.abortus. {ECO:0000269|PubMed:26124143}.
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DR EMBL; AM040264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DOA0; -.
DR SMR; P0DOA0; -.
DR OMA; RWGQFFV; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..945
FT /note="Sensor kinase CckA"
FT /id="PRO_0000436621"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 171..212
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 313..341
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 432..505
FT /note="PAS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 574..797
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 825..941
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 577
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 876
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 945 AA; 103190 MW; D493F02BC05E595E CRC64;
MRPKWCKTTV LASFPRGSAC TARQLKHSAN RIYLDARASV PARRAGILNE DRIELPDDAI
GASAERRSTR DLRKPSRAGI QHERAVGLMS RQTDNTYPKP LVMPKRGPSA ALRLLIVGIL
LMGAAFIYFL FRDQLGDGFA LVLMGVLSMV GVFYLFGAAT GLIQFSQRSD HQDLAHSFMD
TQPEGTVISD PRGQIVYANQ AYARMTGATD ADGIRPLDQV LASEPAASDA IYRLTNAVRD
GLSAQEEVRI SGGLSRGANG SLAPVWYRIK ARALEGGAEF KGPLVAWQVA DISEERAEQE
RFFQELQEAI NHLDHAPAGF FSANPAGRII YLNATLAEWL GVDLTQFTPG SLTLNDIVAG
SGMALIKAVK AEPGTSRNTV IDLDLIKRNG QSLAVRFYHR VQTARDGMPG TTRTIVLDRA
EGDDSSVAQR SAEVRFTRFF NSAPMAIAAV DAEGHTLRTN ARFLDIFSGV VDRDAIDRRV
KLENVVHERD RETFNKALAA AFAGQASISP VDTVLPGNEE RHIRFYMSPV TDLGGEAAEE
AAVISAVETT EQKALENQMA QSQKMQAVGQ LAGGIAHDFN NVLTAIIMSS DLLLTNHRAS
DPSFPDIMNI KQNANRAASL VRQLLAFSRR QTLRPEVLDL TDVLADLRML LARLVGKDIE
LKIDHGRDLW PVKADLGQFE QVAVNLAVNA RDAMPEGGQI TLRTRNIPAA DAAKLHYRDL
PEADYVVFEV EDTGTGIPAD VLEKIFEPFF TTKEVGKGTG LGLSMVYGII KQTGGFIYCD
SEVGKGTTFK IFLPRLIEEK RADDAPVAAK EKKVEKATDL SGSATVLLVE DEDAVRMGGV
RALQSRGYTV HEAASGVEAL EIMEELGGEV DIVVSDVVMP EMDGPTLLRE LRKTHPDIKF
IFVSGYAEDA FARNLPADAK FGFLPKPFSL KQLATTVKEM LEKQD
