ID   A0A399EJV5_9DEIN        Unreviewed;        72 AA.
AC   A0A399EJV5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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   ORFNames=Mlute_02214 {ECO:0000313|EMBL:RIH83369.1};
OS   Meiothermus luteus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=2026184 {ECO:0000313|EMBL:RIH83369.1, ECO:0000313|Proteomes:UP000265800};
RN   [1] {ECO:0000313|EMBL:RIH83369.1, ECO:0000313|Proteomes:UP000265800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52599 {ECO:0000313|EMBL:RIH83369.1,
RC   ECO:0000313|Proteomes:UP000265800};
RA   Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA   Egas C.;
RT   "Meiothermus luteus KCTC 52599 genome sequencing project.";
RL   Submitted (AUG-2018) 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}.
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:RIH83369.1}.
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DR   EMBL; QWKZ01000082; RIH83369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399EJV5; -.
DR   OrthoDB; 9812389at2; -.
DR   Proteomes; UP000265800; Unassembled WGS sequence.
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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088}.
SQ   SEQUENCE   72 AA;  8359 MW;  A28A530EA4D22F3B CRC64;
     MKDLVEYLVK AVVDHPGLVR VDEKRAKEGW VYYVETHHQD KGRVIGRQGR VIEAIRTVVR
     SFSKGRVNVE VR
//