ID   KHPA_LISMO              Reviewed;          76 AA.
AC   P67234; Q92AL2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=lmo1796;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591981; CAC99874.1; -; Genomic_DNA.
DR   PIR; AD1299; AD1299.
DR   RefSeq; NP_465321.1; NC_003210.1.
DR   RefSeq; WP_003728421.1; NZ_CP023861.1.
DR   AlphaFoldDB; P67234; -.
DR   SMR; P67234; -.
DR   STRING; 169963.lmo1796; -.
DR   PaxDb; P67234; -.
DR   EnsemblBacteria; CAC99874; CAC99874; CAC99874.
DR   GeneID; 61189716; -.
DR   GeneID; 67411831; -.
DR   GeneID; 985933; -.
DR   KEGG; lmo:lmo1796; -.
DR   PATRIC; fig|169963.11.peg.1840; -.
DR   eggNOG; COG1837; Bacteria.
DR   HOGENOM; CLU_132074_1_2_9; -.
DR   OMA; AVKMDKR; -.
DR   PhylomeDB; P67234; -.
DR   BioCyc; LMON169963:LMO1796-MON; -.
DR   Proteomes; UP000000817; 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..76
FT                   /note="RNA-binding protein KhpA"
FT                   /id="PRO_0000163229"
FT   DOMAIN          29..76
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
SQ   SEQUENCE   76 AA;  8522 MW;  2213BBF199212A19 CRC64;
     MEELILSIVK PLVDHPEDVV ITPEETDTSL TYKLSVSKED MGRVIGKQGR IAKAIRTLVY
     AVGSKNDKKI RLEIIE