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Database: UniProt
Entry: W1UCC0_CLOBU
LinkDB: W1UCC0_CLOBU
Original site: W1UCC0_CLOBU 
ID   W1UCC0_CLOBU            Unreviewed;        75 AA.
AC   W1UCC0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=Q607_CBUC00030G0074 {ECO:0000313|EMBL:ETI91346.1};
OS   Clostridium butyricum DORA_1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1403941 {ECO:0000313|EMBL:ETI91346.1, ECO:0000313|Proteomes:UP000018876};
RN   [1] {ECO:0000313|EMBL:ETI91346.1, ECO:0000313|Proteomes:UP000018876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_1 {ECO:0000313|Proteomes:UP000018876};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) 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:ETI91346.1}.
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DR   EMBL; AZLX01000030; ETI91346.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1UCC0; -.
DR   PATRIC; fig|1403941.3.peg.576; -.
DR   Proteomes; UP000018876; 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   75 AA;  8388 MW;  92A53C956999E632 CRC64;
     MKELVEYMAK SLVDNPEYVS VNEVNKEQSI ILELKVAPED MGKVIGKQGR IAKAIRTVVK
     AAAVKQHKRV IVEII
//
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