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Database: UniProt
Entry: B2A471_NATTJ
LinkDB: B2A471_NATTJ
Original site: B2A471_NATTJ 
ID   B2A471_NATTJ            Unreviewed;       209 AA.
AC   B2A471;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   OrderedLocusNames=Nther_2931 {ECO:0000313|EMBL:ACB86477.1};
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB86477.1, ECO:0000313|Proteomes:UP000001683};
RN   [1] {ECO:0000313|EMBL:ACB86477.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB86477.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RX   PubMed=21642468; DOI=10.1128/JB.05157-11;
RA   Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA   Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA   Kyrpides N., Wiegel J.;
RT   "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT   Natranaerobius thermophilus JW/NM-WN-LF.";
RL   J. Bacteriol. 193:4023-4024(2011).
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}.
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DR   EMBL; CP001034; ACB86477.1; -; Genomic_DNA.
DR   RefSeq; WP_012449309.1; NC_010718.1.
DR   AlphaFoldDB; B2A471; -.
DR   STRING; 457570.Nther_2931; -.
DR   KEGG; nth:Nther_2931; -.
DR   eggNOG; COG1847; Bacteria.
DR   HOGENOM; CLU_042512_0_1_9; -.
DR   InParanoid; B2A471; -.
DR   OrthoDB; 9794483at2; -.
DR   Proteomes; UP000001683; 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   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:UP000001683};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00867}.
FT   DOMAIN          142..208
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   209 AA;  23567 MW;  5FE7198158BF34C4 CRC64;
     MSQVEVTGKT VEEAVEKGLS ELGIERNLAD IEVIEEPSSG LLGFIGARPA LVKVTKKFDP
     VELASEYLEG ILDRMRIPAT VELKAQANQE IHLEIKGKNL GVIIGKRGQT LDSLQFLTNL
     YLNQKMQGSN HYIILDAENY RDKRKKTLQK LAENLASKVK RTGKKVMLEP MNRYERKIIH
     TSLQDHDGIT TFSEGTEPNR KVVIKLQEK
//
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