ID   KHPA_LISIN              Reviewed;          76 AA.
AC   P67235; Q92AL2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=lin1910;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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; AL596170; CAC97140.1; -; Genomic_DNA.
DR   PIR; AD1671; AD1671.
DR   RefSeq; WP_003728421.1; NC_003212.1.
DR   AlphaFoldDB; P67235; -.
DR   SMR; P67235; -.
DR   STRING; 272626.lin1910; -.
DR   EnsemblBacteria; CAC97140; CAC97140; CAC97140.
DR   GeneID; 61189716; -.
DR   GeneID; 67411831; -.
DR   KEGG; lin:lin1910; -.
DR   eggNOG; COG1837; Bacteria.
DR   HOGENOM; CLU_132074_1_2_9; -.
DR   OMA; AVKMDKR; -.
DR   OrthoDB; 1940160at2; -.
DR   Proteomes; UP000002513; 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   RNA-binding.
FT   CHAIN           1..76
FT                   /note="RNA-binding protein KhpA"
FT                   /id="PRO_0000163227"
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