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Database: UniProt
Entry: R5A969_9FIRM
LinkDB: R5A969_9FIRM
Original site: R5A969_9FIRM 
ID   R5A969_9FIRM            Unreviewed;       205 AA.
AC   R5A969;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=RNA-binding protein KhpB {ECO:0000256|HAMAP-Rule:MF_00867};
DE   AltName: Full=RNA-binding protein EloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN   Name=khpB {ECO:0000256|HAMAP-Rule:MF_00867};
GN   Synonyms=eloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN   ORFNames=BN453_00709 {ECO:0000313|EMBL:CCX39770.1};
OS   Firmicutes bacterium CAG:102.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX39770.1, ECO:0000313|Proteomes:UP000018112};
RN   [1] {ECO:0000313|EMBL:CCX39770.1, ECO:0000313|Proteomes:UP000018112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:102 {ECO:0000313|EMBL:CCX39770.1,
RC   ECO:0000313|Proteomes:UP000018112};
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 KhpA 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_00867}.
CC   -!- SUBUNIT: Forms a complex with KhpA. {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- DOMAIN: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH
CC       and R3H). {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_00867}.
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:CCX39770.1}.
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DR   EMBL; CAWG010000041; CCX39770.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5A969; -.
DR   STRING; 1262998.BN453_00709; -.
DR   Proteomes; UP000018112; 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; cd02414; KH-II_Jag; 1.
DR   CDD; cd02644; R3H_jag; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.30.30.80; probable RNA-binding protein from clostridium symbiosum atcc 14940; 1.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   HAMAP; MF_00867; KhpB; 1.
DR   InterPro; IPR038008; Jag_KH.
DR   InterPro; IPR038247; Jag_N_dom_sf.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR039247; KhpB.
DR   InterPro; IPR032782; KhpB_N.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR034079; R3H_KhpB.
DR   NCBIfam; NF041568; Jag_EloR; 1.
DR   PANTHER; PTHR35800; PROTEIN JAG; 1.
DR   PANTHER; PTHR35800:SF1; RNA-BINDING PROTEIN KHPB; 1.
DR   Pfam; PF14804; Jag_N; 1.
DR   Pfam; PF13083; KhpA-B_KH; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM01245; Jag_N; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00867};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00867};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00867};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00867};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018112};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00867}.
FT   DOMAIN          140..205
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          5..55
FT                   /note="Jag_N domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00867"
SQ   SEQUENCE   205 AA;  23345 MW;  91137B1558625747 CRC64;
     MEEIRKSAKT VDDAIAAALA ELGATREEVD ITVIDEGSKG FLGMFGSKDA VVLVKKNFNP
     EKEAETFLKE VFLSMGLIVK IKTEQKDKHL YIDLTGDDMG ILIGKRGQTL DALQYLVNLV
     VNKKSPYYIS VMLDTENYRQ RRKETLESLA FNLAKKVKHT KRNVVLEPMN PYERRIIHSA
     LQNDRFVTTY SEGEEPYRNV VITLK
//
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