ID A5N6T9_CLOK5 Unreviewed; 269 AA.
AC A5N6T9;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Extracellular amino acid-binding protein {ECO:0000313|EMBL:EDK33020.1};
GN OrderedLocusNames=CKL_0978 {ECO:0000313|EMBL:EDK33020.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33020.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK33020.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000256|ARBA:ARBA00010333, ECO:0000256|RuleBase:RU003744}.
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DR EMBL; CP000673; EDK33020.1; -; Genomic_DNA.
DR RefSeq; WP_012101350.1; NC_009706.1.
DR AlphaFoldDB; A5N6T9; -.
DR STRING; 431943.CKL_0978; -.
DR KEGG; ckl:CKL_0978; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_5_9; -.
DR Proteomes; UP000002411; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR CDD; cd13530; PBP2_peptides_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR35936:SF19; ABC TRANSPORTER ARGININE-BINDING PROTEIN ARTJ-RELATED; 1.
DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002411};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039330989"
FT DOMAIN 44..266
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT DOMAIN 44..265
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
SQ SEQUENCE 269 AA; 29753 MW; CD3163C2D77AED5A CRC64;
MRNFKKAIVS LVMIIFTVAL FTGCGNNSGN ETQNSLEKVK KAGVLKIGLE DSFPPMEFRD
SKNVLQGFDV DMANAIGEKL GVKTEFVGTE FNGIVLALKS GKFDVIISGL SIDEDRKKEI
DFSEPYIENS QIIITKVEND TIKTSKDLEG KIVGVGLGTT SEKVAKELTG LKEVKKYDKT
TEELQDLLIG RIDAVIVDEP VGKYYISADD KKGKYTVLNE KLTSEPMGIG FRKGDKELEE
AVQRAVNELK EDGTMSKISA KWFGEDIYK
//
