ID A0A1J4XCJ5_9PROT Unreviewed; 718 AA.
AC A0A1J4XCJ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Response regulatory domain-containing protein {ECO:0000259|PROSITE:PS50110};
GN ORFNames=AUJ55_03985 {ECO:0000313|EMBL:OIO59123.1};
OS Proteobacteria bacterium CG1_02_64_396.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1805333 {ECO:0000313|EMBL:OIO59123.1, ECO:0000313|Proteomes:UP000192865};
RN [1] {ECO:0000313|EMBL:OIO59123.1, ECO:0000313|Proteomes:UP000192865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_64_396 {ECO:0000313|EMBL:OIO59123.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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:OIO59123.1}.
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DR EMBL; MNWR01000032; OIO59123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4XCJ5; -.
DR STRING; 1805333.AUJ55_03985; -.
DR Proteomes; UP000192865; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR PANTHER; PTHR30258:SF1; PROTEIN TRANSPORT PROTEIN HOFB HOMOLOG; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 594..710
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 643
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 718 AA; 79918 MW; E72E5BD2AEF99C3A CRC64;
MGNHLVGQGL ITVEQWEKVR GLNGRAMIQT LVQDQKVPER DLVTKLASFY HVPFIDLERF
PVRAEMAEQV PQKAAMKYKI VPLQEHNGQL LVAMIDPLDL KAVDEIRFTL NRPIKGVFAT
PSAIQKRLEA IYGSSADDAM AGLSESLEDA EVREDDGSEE QEEDAESLAR AASDSPVIKM
VNGILAEAIK KGVSDIHIEP TETQLVVRYR IDGKLRPIFK LQKQYSKPVA SRIKIISNLD
ISNTRTPQDG RTKLKVGQKS FDMRVSTLPT YFGEKVVIRI LDKGAINLGL EVLGFNKGEL
DLMQKCAGYP QGMILVTGPT GSGKTTTLYS VLNYLNSEDT NIITVEDPVE FQIKGINQVP
INPAAGMTFA AALKSILRQD PNVIMVGEIR DLETAETAMH ASQTGHMVLS TLHTNGAAET
IGRLVEMGLE PYQISSSLTM VEAQRLLRKI CPNCKVPDDS LTPQLRQKYN IPEEIVFYHG
KGCDTCGGSG NKGRIGAYEV LFLNDAIKEM ISRRATELEL RDTGRDQGMM TMFEDGLVKV
MRGLVSWGEF IDVLPEPTDL EIDGSYLMKA YLQAYEKRVD VRYSEQNQER ENNLILVVDD
SATIRNLVRF ILTNDGFEVL EAEDGQAALQ VLRKQRPDLI MTDREMPKMD GLELIKKLRS
SASTADIPII MLTSRREEDS EVEGLSAGAD DYIGKPIEPA KLAARVRKVL KLYKRMQA
//