ID Q5SJH4_THET8 Unreviewed; 72 AA.
AC Q5SJH4;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=RNA-binding protein KhpA {ECO:0000256|HAMAP-Rule:MF_00088};
DE AltName: Full=KH-domain protein A {ECO:0000256|HAMAP-Rule:MF_00088};
GN Name=khpA {ECO:0000256|HAMAP-Rule:MF_00088};
GN OrderedLocusNames=TTHA1034 {ECO:0000313|EMBL:BAD70857.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70857.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD70857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB8 {ECO:0000313|EMBL:BAD70857.1};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A probable RNA chaperone. Forms a complex with KhpB which
CC binds to cellular RNA and controls its expression. Plays a role in
CC peptidoglycan (PG) homeostasis and cell length regulation.
CC {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SUBUNIT: Forms a complex with KhpB. {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088}.
CC -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC {ECO:0000256|HAMAP-Rule:MF_00088}.
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DR EMBL; AP008226; BAD70857.1; -; Genomic_DNA.
DR RefSeq; WP_011173114.1; NC_006461.1.
DR RefSeq; YP_144300.1; NC_006461.1.
DR AlphaFoldDB; Q5SJH4; -.
DR EnsemblBacteria; BAD70857; BAD70857; BAD70857.
DR GeneID; 3169162; -.
DR KEGG; ttj:TTHA1034; -.
DR PATRIC; fig|300852.9.peg.1014; -.
DR eggNOG; COG1837; Bacteria.
DR HOGENOM; CLU_132074_1_0_0; -.
DR PhylomeDB; Q5SJH4; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd22533; KH-II_YlqC-like; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_00088; KhpA; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR020627; KhpA.
DR PANTHER; PTHR34654:SF1; RNA-BINDING PROTEIN KHPA; 1.
DR PANTHER; PTHR34654; UPF0109 PROTEIN SCO5592; 1.
DR Pfam; PF13083; KhpA-B_KH; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00088};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00088};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00088};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ SEQUENCE 72 AA; 8212 MW; C391DEC59E02D973 CRC64;
MKDVVEYLVR YLVDRPEAVR VQVRRGKEGT VYLVEVAPED KGRLIGKGGR VIESLRTVVR
AYAKRKVGVE VR
//
