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Database: UniProt
Entry: R6C099_9CLOT
LinkDB: R6C099_9CLOT
Original site: R6C099_9CLOT 
ID   R6C099_9CLOT            Unreviewed;        75 AA.
AC   R6C099;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=BN687_00846 {ECO:0000313|EMBL:CDA68865.1};
OS   Clostridium sp. CAG:510.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262816 {ECO:0000313|EMBL:CDA68865.1, ECO:0000313|Proteomes:UP000018120};
RN   [1] {ECO:0000313|EMBL:CDA68865.1, ECO:0000313|Proteomes:UP000018120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:510 {ECO:0000313|Proteomes:UP000018120};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA68865.1}.
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DR   EMBL; CBCI010000078; CDA68865.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6C099; -.
DR   STRING; 1262816.BN687_00846; -.
DR   Proteomes; UP000018120; 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.
DR   PROSITE; PS50084; KH_TYPE_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000018120};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088, ECO:0000256|PROSITE-
KW   ProRule:PRU00117}.
SQ   SEQUENCE   75 AA;  8069 MW;  30A0C4D350B1998D CRC64;
     MKELVEVIAK ALVDNPDEVV VTEKTEGKNV TVELHVAASD MGKVIGKQGR IAKAIRSVVK
     AASSKDNKRV DVEII
//
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