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Database: UniProt
Entry: I3E4V3_BACMT
LinkDB: I3E4V3_BACMT
Original site: I3E4V3_BACMT 
ID   I3E4V3_BACMT            Unreviewed;        76 AA.
AC   I3E4V3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=PB1_01225 {ECO:0000313|EMBL:EIJ81524.1};
OS   Bacillus methanolicus PB1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ81524.1, ECO:0000313|Proteomes:UP000010523};
RN   [1] {ECO:0000313|EMBL:EIJ81524.1, ECO:0000313|Proteomes:UP000010523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1 {ECO:0000313|EMBL:EIJ81524.1,
RC   ECO:0000313|Proteomes:UP000010523};
RX   PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA   Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA   Brautaset T.;
RT   "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT   Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT   Glutamate from Methanol.";
RL   Appl. Environ. Microbiol. 78:5170-5181(2012).
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:EIJ81524.1}.
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DR   EMBL; AFEU01000001; EIJ81524.1; -; Genomic_DNA.
DR   RefSeq; WP_003350226.1; NZ_AFEU01000001.1.
DR   AlphaFoldDB; I3E4V3; -.
DR   STRING; 997296.PB1_01225; -.
DR   PATRIC; fig|997296.3.peg.293; -.
DR   eggNOG; COG1837; Bacteria.
DR   OrthoDB; 9812389at2; -.
DR   Proteomes; UP000010523; 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|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00088};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, 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   76 AA;  8559 MW;  9361DC001E98C8CC CRC64;
     MKELIETIVK PLVDFPEDVQ VNVLEEDHRV TYQLSVNKND MGKVIGKQGR VANAIRTVVY
     AAGSSQQKKI FLEISE
//
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