ID   KHPB_CLOSY              Reviewed;         222 AA.
AC   D0VX24;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=RNA-binding protein KhpB {ECO:0000255|HAMAP-Rule:MF_00867};
DE   AltName: Full=RNA-binding protein EloR {ECO:0000255|HAMAP-Rule:MF_00867};
GN   Name=khpB {ECO:0000255|HAMAP-Rule:MF_00867};
GN   Synonyms=eloR {ECO:0000255|HAMAP-Rule:MF_00867};
OS   Clostridium symbiosum (Bacteroides symbiosus).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1512;
RN   [1] {ECO:0000312|PDB:3GKU, ECO:0007744|PDB:3GKU}
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 1-208, SUBUNIT, AND DOMAIN.
RA   Tan K., Keigher L., Jedrzejczak R., Babnigg G., Joachimiak A.;
RT   "The crystal structure of a probable RNA-binding protein from Clostridium
RT   symbiosum ATCC 14940.";
RL   Submitted (MAR-2009) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_00867}.
CC   -!- SUBUNIT: Forms a complex with KhpA (By similarity). Homodimer or
CC       homotrimer (Ref.1). {ECO:0000255|HAMAP-Rule:MF_00867,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00867}.
CC   -!- DOMAIN: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH
CC       and R3H). {ECO:0000255|HAMAP-Rule:MF_00867}.
CC   -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00867}.
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DR   PDB; 3GKU; X-ray; 2.95 A; A/B/C=1-208.
DR   PDBsum; 3GKU; -.
DR   EvolutionaryTrace; D0VX24; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd02414; jag_KH; 1.
DR   CDD; cd02644; R3H_jag; 1.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   Gene3D; 3.30.30.80; -; 1.
DR   Gene3D; 3.30.300.20; -; 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   PANTHER; PTHR35800; PTHR35800; 1.
DR   Pfam; PF14804; Jag_N; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM01245; Jag_N; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; SSF82708; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell shape; Cell wall biogenesis/degradation; Chaperone;
KW   Cytoplasm; RNA-binding.
FT   CHAIN           1..222
FT                   /note="RNA-binding protein KhpB"
FT                   /id="PRO_0000454541"
FT   DOMAIN          54..133
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00867"
FT   DOMAIN          138..204
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00867"
FT   REGION          2..51
FT                   /note="Jag_N domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00867"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           59..73
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           107..124
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           139..161
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   HELIX           172..181
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          186..195
FT                   /evidence="ECO:0007829|PDB:3GKU"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:3GKU"
SQ   SEQUENCE   222 AA;  25549 MW;  B64FA28EB0C0B055 CRC64;
     MDMVTVTAKT VEEAVTKALI ELQTTSDKLT YEIVEKGSAG FLGIGSKPAI IRAKRKETLQ
     DKAIEFLEQV FDAMNMAVDI SVEYNETEKE MNVNLKGDDM GILIGKRGQT LDSLQYLVSL
     VVNKSSSDYI RVKLDTENYR ERRKETLETL AKNIAYKVKR TKRSVSLEPM NPYERRIIHA
     ALQNDKYVVT RSDGEEPFRH VIISLKRENR RDRNDRSDRN EK