ID S3MUX0_9GAMM Unreviewed; 431 AA.
AC S3MUX0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN ORFNames=F945_02582 {ECO:0000313|EMBL:EPF71550.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71550.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF71550.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71550.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of a two-component regulatory system.
CC {ECO:0000256|RuleBase:RU364088}.
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|RuleBase:RU364088};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU364088}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EPF71550.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATGI01000032; EPF71550.1; -; Genomic_DNA.
DR AlphaFoldDB; S3MUX0; -.
DR STRING; 632955.GCA_000829675_01342; -.
DR PATRIC; fig|421052.3.peg.2524; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_6_6; -.
DR Proteomes; UP000014568; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR048590; CusS-like_sensor.
DR InterPro; IPR006290; CztS_silS_copS.
DR InterPro; IPR003660; HAMP_dom.
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 NCBIfam; TIGR01386; cztS_silS_copS; 1.
DR PANTHER; PTHR45436:SF17; SENSOR HISTIDINE KINASE CUSS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF21085; CusS; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|RuleBase:RU364088};
KW Cell inner membrane {ECO:0000256|RuleBase:RU364088};
KW Cell membrane {ECO:0000256|RuleBase:RU364088};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364088};
KW Membrane {ECO:0000256|RuleBase:RU364088};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364088};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000014568};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364088};
KW Transmembrane {ECO:0000256|RuleBase:RU364088};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364088};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|RuleBase:RU364088}.
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT DOMAIN 158..211
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 219..431
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 431 AA; 49400 MW; D5EE0DBA188A27A7 CRC64;
MGAVIHHLVL EHFDQQDKKV LDGKVELIQH LLESQQFSDQ QFHAALQQTM IGHDELMVMV
QRENQQFLFN SFAHLDAGRP IKVLNQNWFE WEITDRTYRG YVINKPFVRN MGQETFLITV
AIDNTAHHLF MLQFSRQLKI IGLLGMLGLV IFAWLAVRRG LNPIVKMSHV VKGITAQNLT
QRLDLDHIPI ELKSLATEFN QMLTRLEKAL DKLSNFSSDL AHEIRTPINV LMTQTQVCLS
QTRPIHDYQE VLFSNLEEFE RLAKMTADLL FLAKAEHQLE LIDRAPIDLQ HEMANLLDYY
DALASEKGMQ LLHHGEATIS GDVQMLRRAL SNLIANAIQY GLANTPIRID YQQSAKQVVL
NIENQAETLT SAQLDNLFDR FYRADISRQK TIEGTGLGLA ITQSILELHQ AKIEVQSQEG
WVRFSLVFPV D
//
