ID A0A1I3IXV4_9GAMM Unreviewed; 914 AA.
AC A0A1I3IXV4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phosphotransferase RcsD {ECO:0000256|HAMAP-Rule:MF_00980};
DE EC=2.7.2.- {ECO:0000256|HAMAP-Rule:MF_00980};
DE AltName: Full=Phosphotransfer intermediate RcsD {ECO:0000256|HAMAP-Rule:MF_00980};
GN Name=rcsD {ECO:0000256|HAMAP-Rule:MF_00980};
GN ORFNames=SAMN05421680_10221 {ECO:0000313|EMBL:SFI52794.1};
OS Xenorhabdus mauleonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351675 {ECO:0000313|EMBL:SFI52794.1, ECO:0000313|Proteomes:UP000198919};
RN [1] {ECO:0000313|Proteomes:UP000198919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17908 {ECO:0000313|Proteomes:UP000198919};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsD is a phosphotransfer intermediate
CC between the sensor kinase RcsC and the response regulator RcsB. It
CC acquires a phosphoryl group from RcsC and transfers it to RcsB.
CC {ECO:0000256|HAMAP-Rule:MF_00980}.
CC -!- SUBUNIT: Interacts with RcsC and RcsB. {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00980}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
CC -!- PTM: Phosphorylated by RcsC. {ECO:0000256|HAMAP-Rule:MF_00980}.
CC -!- SIMILARITY: Belongs to the RcsD family. {ECO:0000256|HAMAP-
CC Rule:MF_00980}.
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DR EMBL; FORG01000002; SFI52794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3IXV4; -.
DR STRING; 351675.SAMN05421680_10221; -.
DR OrthoDB; 6414457at2; -.
DR Proteomes; UP000198919; 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:0009927; F:histidine phosphotransfer kinase activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProt.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR CDD; cd00088; HPT; 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 Gene3D; 3.40.50.11620; Phosphotransferase RcsD, RcsD-ABL domain; 1.
DR HAMAP; MF_00980; RcsD; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR030861; Ptransferase_RcsD.
DR InterPro; IPR032306; RcsD_ABL.
DR InterPro; IPR038616; RcsD_ABL_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 1.
DR Pfam; PF16359; RcsD_ABL; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00980};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00980, ECO:0000313|EMBL:SFI52794.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00980};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00980}; Transferase {ECO:0000256|HAMAP-Rule:MF_00980};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00980};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00980};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|HAMAP-Rule:MF_00980}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00980"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00980"
FT DOMAIN 449..667
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 822..914
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 861
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00980,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 914 AA; 104744 MW; 351E636A5B82ED15 CRC64;
MSKQPPIKPS AIPRFYTLFV TLLFTSLFLF GYNYFDIWLM EKKYAISSVT AKMRLQIGDY
RYHANHIFEQ SNTLPVSSQN SASLIKLRPD AYWLENRNQS VDAIIFGQFN DSSVQLAQQL
SNYLGILWGS RNEYLSMYYL NGKDNNLLLV TNHSVLKPEI KLKESYLTRT PDIRRSEMLD
QSITLEEKES ISPINVLRSE NLYFYTYKAA FNTVGQLTTV IAFDLPINNL LPVDMSPANF
RLQATNLHDF DNSNNVDVSL NGFWLEFSQP LKMMPYKLVY QVPLKTLIAD LLFRNVWLLL
SILLFFLFSL SGIFYIRRRY IAPNASMGHE LKIKNALNKD IIANIPVGLL VYDFESNQMV
IYNKIAEKLI PHLDLNKVKT VAQQHHGVIQ TSIDEAIYEV KMYNNDLLPE TYLFLLQDKD
QEVMINKRLQ LAHREYDKSI QARRSMLSNI NNEIKIPIKG MNDIAVQLKQ LSQDENELKL
LDKLLAKSEY ITEWVDNISL LNGLELGDWQ PVNEVFSLSS RLENILKASL ATLNAKGLRV
YYHFNIPHES LFIGDGYALS KIVTLLFNYA MTTTSYGKIS LTVNSSGKYD NHIQIELVDS
GSGLSEKDLM SLNYPFLNQS AEDKYSTNSG MTFYLCNQLC KRMDGSLEIK SKLSLGTHYV
INLPLVQHDE ENSETPRLLE GVTALIDINN PEISKIIHTY LDDYGATYFV KGKENVTEEC
DIILTDKRYK EKKSTILLVG SLAGFERVKP GLIKCNYNFV DSVINAISLL IEENFSLDES
RETPEFTQLT YDLSDNTNAV ENIDLFASGD SNIWNIIKNC QIQLANSDYR ELFIETVPMD
ITKLYTDIEQ YDLVSLSQTV HRLKGVFAML ELKFLRSSCE ALEKHIADNN EVEIKNSISL
IDSFVTKLLQ QGNQ
//
