ID A9I798_BORPD Unreviewed; 313 AA.
AC A9I798;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=ABC transporter permease protein {ECO:0000313|EMBL:CAP44389.1};
GN OrderedLocusNames=Bpet4041 {ECO:0000313|EMBL:CAP44389.1};
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:CAP44389.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP44389.1, 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
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DR EMBL; AM902716; CAP44389.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I798; -.
DR STRING; 94624.Bpet4041; -.
DR KEGG; bpt:Bpet4041; -.
DR eggNOG; COG0601; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF6; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 99..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 235..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 281..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 95..300
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 313 AA; 34146 MW; C196621F82CE8166 CRC64;
MLAFILRRLL ATIPVLVLVA VVVFAILRLS PGDPAVIMAG DGATPERIEQ IRQVMGLDQP
LFKQFFLWAG RLVQGDIGTS LMSGVPVRQL IGQRLEPSLS LALLTLVFTL AVAIPLGILA
AWRQGRLLDR MVMGFSVLGF SVPVFVTAYL LIWAFAIELD WFKVQGYTPL SAGFWPFLHR
LILPALALST IYVALIARIT RTSVIEVMGE DFIRTARAKG LGETGVLLGH ALRNAAVPIA
TVVGVGIALL ISGVVVTESV FNIPGLGRLV VEAVLARDYP VIQGLTLFFA FVYVFINLVV
DCAYTLFDPR IRY
//
