ID A9IMV4_BORPD Unreviewed; 515 AA.
AC A9IMV4;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Oligopeptide transport system substrate-binding protein {ECO:0000313|EMBL:CAP42755.1};
GN Name=appA {ECO:0000313|EMBL:CAP42755.1};
GN OrderedLocusNames=Bpet2412 {ECO:0000313|EMBL:CAP42755.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42755.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42755.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000256|ARBA:ARBA00005695}.
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DR EMBL; AM902716; CAP42755.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IMV4; -.
DR STRING; 94624.Bpet2412; -.
DR KEGG; bpt:Bpet2412; -.
DR eggNOG; COG0747; Bacteria.
DR OMA; WDTLIYR; -.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd08515; PBP2_NikA_DppA_OppA_like_10; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290:SF38; DIPEPTIDE-BINDING PROTEIN; 1.
DR PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002738922"
FT DOMAIN 81..438
FT /note="Solute-binding protein family 5"
FT /evidence="ECO:0000259|Pfam:PF00496"
SQ SEQUENCE 515 AA; 57649 MW; 8CA5320147848653 CRC64;
MAECRVSFVA SLSFRLPAAL LLAGALAAQP AWAGKQDDTL RMAYDQAPES VDPYFNNVRI
GVIIAANVWD TLLYRDPLTN EYKGQLAKSW KQVDDKTLEF ELREGVKFHN GEEFDADSVV
YTLNFVADPK NKATTQQNVR WIDKVEKLGK YKVRLTTKEP FPAAKEYLST TVAIHPAKYY
AEVGPQGMNA KPVGTGPYKV TEYVPGKSIT LQANKDYFKD SPKAQPKIGK VVIRFIPDRQ
TQMAEVISGG EDFIMHVPKD QAEQLKTLPQ LQVKSGNTMR IVFMQMNILD NTPAPQLKDE
RVRKAILHAI DREAIIKNIV GEGAEVLNTI CTPSQVGCTD EGAPVYKYDP ALSKKLLAEA
GYPDGFDIDI VAYRERNQTE AIINYLQAVG IRAKLNFLQY AAMRDMIRGG KASLTHQTWG
SNLVNDVSAS TPVYFSFGKD DITHDPKVRE LLDKGDHTID SAARDAAYKQ ALTMIAEHAY
AAPLWSLPVY YVASKDVDFT PYPDELVRFW DMSWK
//