ID   KHPA_CLOAB              Reviewed;          75 AA.
AC   Q97I96;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CA_C1756;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(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; AE001437; AAK79722.1; -; Genomic_DNA.
DR   PIR; G97116; G97116.
DR   RefSeq; NP_348382.1; NC_003030.1.
DR   RefSeq; WP_010965063.1; NC_003030.1.
DR   AlphaFoldDB; Q97I96; -.
DR   SMR; Q97I96; -.
DR   STRING; 272562.CA_C1756; -.
DR   EnsemblBacteria; AAK79722; AAK79722; CA_C1756.
DR   GeneID; 44998251; -.
DR   KEGG; cac:CA_C1756; -.
DR   PATRIC; fig|272562.8.peg.1960; -.
DR   eggNOG; COG1837; Bacteria.
DR   HOGENOM; CLU_132074_1_0_9; -.
DR   OMA; AVKMDKR; -.
DR   OrthoDB; 1940160at2; -.
DR   Proteomes; UP000000814; 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.
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_0000163222"
FT   DOMAIN          29..75
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
SQ   SEQUENCE   75 AA;  8170 MW;  A68E2113FA4FE2DE CRC64;
     MKQLLETIAK SLVDCPDEVQ VSEVTGEQSI ILELKVAPED MGKVIGKQGR IAKAIRTVIK
     AAAVKENKRV VVEII