ID   KHPA_THEMA              Reviewed;          75 AA.
AC   Q9X1Q3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=RNA-binding protein KhpA {ECO:0000255|HAMAP-Rule:MF_00088};
DE   AltName: Full=KH-domain protein A {ECO:0000255|HAMAP-Rule:MF_00088};
GN   Name=khpA {ECO:0000255|HAMAP-Rule:MF_00088}; OrderedLocusNames=TM_1567;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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:0000255|HAMAP-Rule:MF_00088}.
CC   -!- SUBUNIT: Forms a complex with KhpB. {ECO:0000255|HAMAP-Rule:MF_00088}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00088}.
CC   -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00088}.
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DR   EMBL; AE000512; AAD36634.1; -; Genomic_DNA.
DR   PIR; H72236; H72236.
DR   RefSeq; NP_229367.1; NC_000853.1.
DR   RefSeq; WP_004081981.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X1Q3; -.
DR   SMR; Q9X1Q3; -.
DR   STRING; 243274.THEMA_06445; -.
DR   EnsemblBacteria; AAD36634; AAD36634; TM_1567.
DR   KEGG; tma:TM1567; -.
DR   eggNOG; COG1837; Bacteria.
DR   InParanoid; Q9X1Q3; -.
DR   OMA; AVKMDKR; -.
DR   OrthoDB; 1940160at2; -.
DR   Proteomes; UP000008183; 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   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; PTHR34654; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Chaperone; Cytoplasm;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..75
FT                   /note="RNA-binding protein KhpA"
FT                   /id="PRO_0000163236"
FT   DOMAIN          29..75
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
SQ   SEQUENCE   75 AA;  8494 MW;  0AB23DD5DE3DB16E CRC64;
     MKELLEKILR GIVKHPEEVV VMEFDEEGKK VYEIVVNEED VGQVIGKDGR TIKSLKILLS
     ALMGDSKEIT IKVVR