ID D1P5J0_9GAMM Unreviewed; 927 AA.
AC D1P5J0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Sensor histidine kinase RcsC {ECO:0000256|HAMAP-Rule:MF_00979};
DE EC=2.7.13.3 {ECO:0000256|HAMAP-Rule:MF_00979};
GN Name=rcsC {ECO:0000256|HAMAP-Rule:MF_00979};
GN ORFNames=PROVRUST_07498 {ECO:0000313|EMBL:EFB71314.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB71314.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB71314.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB71314.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsC functions as a membrane-
CC associated protein kinase that phosphorylates RcsD in response to
CC environmental signals. The phosphoryl group is then transferred to the
CC response regulator RcsB. {ECO:0000256|HAMAP-Rule:MF_00979}.
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 ECO:0000256|HAMAP-Rule:MF_00979};
CC -!- SUBUNIT: Interacts with RcsD. {ECO:0000256|HAMAP-Rule:MF_00979}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00979}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00979}.
CC -!- PTM: Autophosphorylated. Activation probably requires a transfer of a
CC phosphate group from a His in the transmitter domain to an Asp in the
CC receiver domain. {ECO:0000256|HAMAP-Rule:MF_00979}.
CC -!- SIMILARITY: Belongs to the RcsC family. {ECO:0000256|HAMAP-
CC Rule:MF_00979}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00979}.
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:EFB71314.1}.
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DR EMBL; ABXV02000040; EFB71314.1; -; Genomic_DNA.
DR AlphaFoldDB; D1P5J0; -.
DR STRING; 500637.PROVRUST_07498; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_15_6_6; -.
DR Proteomes; UP000005512; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.40.50.10970; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00979; RcsC; 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; IPR030856; RcsC.
DR InterPro; IPR038388; RcsC_C_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR019017; Sig_transdc_His_kin_a/b-loop_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF09456; RcsC; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS51426; ABL; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00979};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00979};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00979};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00979}; Transferase {ECO:0000256|HAMAP-Rule:MF_00979};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00979};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00979};
KW Two-component regulatory system {ECO:0000256|HAMAP-Rule:MF_00979}.
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979"
FT DOMAIN 459..674
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 687..788
FT /note="ABL"
FT /evidence="ECO:0000259|PROSITE:PS51426"
FT DOMAIN 809..923
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 462
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979"
FT MOD_RES 858
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00979,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 927 AA; 105428 MW; DD3AD1EDB3C6C996 CRC64;
MLWGMGLFIT LFFLYMQFNE SKSDLRQQFH SGYDNLQTYI QQTSTTLRLI HSMTEQQKVK
YEEYQQKIDV QPESISMPTS TSYNLYPLIP TADCESFKKN TKNYLAAFEQ LNYFWKDSIG
APQGLNHVFI TGTISQCMMD YPTRSAVTDL EGLKRIAYET TRSYKAFKMQ GQEHNLYAIA
HGAQSDNGQI YVLMPIYSRN LLVGFIGVER AINLNQFNLR NNKAVDIMIV NSSNQPILFS
SSDANIKASP LLVASEQNYF GFNSDYTKLF FKKRLVPSQL TVIYSISTSH LIENIKNSIF
YAIFLNVFSG GLIFFLIWLL ERKMLEPAEN TAIRLEEHEQ FNHKIVASAP VGIIILRLSD
GGNILSNELA HNYFRLLNDE DKQRILSIIR QKSSNYIDVV TTSGTHLQIS FVNSRYQNED
VAICVLIDIS IRVQMEKSLQ DVADAAEQAN QAKSMFLATV SHELRTPLYG IIGNIELLQR
YDLSDKAVRL VSTMDNSSSL LLQIISDILD FSKIESEQLK IENKSFNCRD VFAFVLANYV
PLASKKHISL YSYVEPNIPD LMLSDAVRLQ QVISNIVNNS IKFTDSGFVM LHVWKDSNYL
KIEIKDSGIG MTPAVVMQLF DPFFQVYDQN NGHKGTGLGL AICEKLINLM DGDIAVNSQA
GLGSTFTIRI PLYGQKYLEQ VIPEYRKNYR IAVTCQNTFL MNFLIRLLKH HHFNVVESQH
IEDNEHVDLV ITDHQHEVAI AGENLIRLLD LYTGELIETQ PNDWSYNTYQ LDKLPMLIDK
IIVKVAQNSK ELFNDENKQE TDIALNEFKI LIVDDHPINR MLLVEQLTSI GFSTGTAVDG
LDALKYLEHH QVDIVLSDVN MPNMDGYQLS GALRKTGFSQ PIVALTANAM AEEKQRCLDA
GMNDCLSKPT SIRVLREALV KYVKPNV
//
