DPPD_CALS4
ID DPPD_CALS4 Reviewed; 326 AA.
AC Q8RDH4;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dipeptide transport ATP-binding protein DppD {ECO:0000250|UniProtKB:A2RI77};
DE EC=7.4.2.9 {ECO:0000250|UniProtKB:A2RI77};
GN Name=dppD {ECO:0000303|PubMed:23385461};
GN OrderedLocusNames=TTE0057 {ECO:0000312|EMBL:AAM23365.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
RN [2] {ECO:0007744|PDB:4FWI}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH ATP; MAGNESIUM AND
RP IRON-SULFUR (4FE-4S), ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=23385461; DOI=10.1107/s0907444912045180;
RA Li X., Zhuo W., Yu J., Ge J., Gu J., Feng Y., Yang M., Wang L., Wang N.;
RT "Structure of the nucleotide-binding domain of a dipeptide ABC transporter
RT reveals a novel iron-sulfur cluster-binding domain.";
RL Acta Crystallogr. D 69:256-265(2013).
CC -!- FUNCTION: Part of the ABC transporter Dpp involved in dipeptide
CC transport. Responsible for energy coupling to the transport system.
CC {ECO:0000250|UniProtKB:A2RI77}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23120, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90799, ChEBI:CHEBI:456216; EC=7.4.2.9;
CC Evidence={ECO:0000250|UniProtKB:A2RI77};
CC -!- ACTIVITY REGULATION: The C-terminal iron-sulfur cluster may stabilize
CC the structure of the C-terminal loops and may function in the
CC regulation of the transport process. {ECO:0000269|PubMed:23385461}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: Contains an N-terminal conserved nucleotide-binding domain and
CC a C-terminal domain bound with a [4Fe-4S] cluster. The C-terminal
CC domain forms a stable loop region and interacts with the N-terminal
CC domain. {ECO:0000269|PubMed:23385461}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AE008691; AAM23365.1; -; Genomic_DNA.
DR RefSeq; WP_009610546.1; NC_003869.1.
DR PDB; 4FWI; X-ray; 2.89 A; B=1-326.
DR PDBsum; 4FWI; -.
DR AlphaFoldDB; Q8RDH4; -.
DR SMR; Q8RDH4; -.
DR STRING; 273068.TTE0057; -.
DR EnsemblBacteria; AAM23365; AAM23365; TTE0057.
DR KEGG; tte:TTE0057; -.
DR eggNOG; COG0444; Bacteria.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; VACWLVE; -.
DR OrthoDB; 1101128at2; -.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Cell membrane; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Nucleotide-binding; Peptide transport;
KW Protein transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..326
FT /note="Dipeptide transport ATP-binding protein DppD"
FT /id="PRO_0000452197"
FT DOMAIN 5..255
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 44..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 298
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:23385461,
FT ECO:0007744|PDB:4FWI"
FT STRAND 3..16
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4FWI"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:4FWI"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:4FWI"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:4FWI"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4FWI"
SQ SEQUENCE 326 AA; 36361 MW; C3BAE78BDC12F15A CRC64;
MSIIIRVEDL RAVYLVREGT IKAADGISLD ILENSVTAIV GESASGKSTI IEAMTKTLPP
NGRILSGRVL YKGKDLLTMR EEELRKIRWK EIALVPQAAQ QSLNPTMKVI EHFKDTVEAH
GVRWSHSELI EKASEKLRMV RLNPEAVLNS YPLQLSGGMK QRVLIALALL LDPVVLILDE
PTSALDVLTQ AHIIQLLKEL KKMLKITLIF VTHDIAVAAE LADKVAVIYG GNLVEYNSTF
QIFKNPLHPY TRGLINSIMA VNADMSKVKP IPGDPPSLLN PPSGCRFHPR CEYAMEICKK
EKPKWIRLDG EAHVACHLYE EGRPLK
