FBPB1_HAEIN
ID FBPB1_HAEIN Reviewed; 632 AA.
AC Q57341; O05010;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative ferric transport system permease protein FbpB 1;
GN Name=fbpB1; Synonyms=afuB; OrderedLocusNames=HI_0129;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J.,
RA Hickey E., Dodson R., Gwinn M.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1)
CC involved in Fe(3+) ions import. Probably responsible for the
CC translocation of the substrate across the membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FbpC),
CC two transmembrane proteins (FbpB) and a solute-binding protein (FbpA).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. FbpB subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC21802.1; -; Genomic_DNA.
DR PIR; H64049; H64049.
DR RefSeq; NP_438299.1; NC_000907.1.
DR RefSeq; WP_010868940.1; NC_000907.1.
DR AlphaFoldDB; Q57341; -.
DR SMR; Q57341; -.
DR STRING; 71421.HI_0129; -.
DR EnsemblBacteria; AAC21802; AAC21802; HI_0129.
DR KEGG; hin:HI_0129; -.
DR PATRIC; fig|71421.8.peg.132; -.
DR eggNOG; COG1178; Bacteria.
DR HOGENOM; CLU_021838_1_1_6; -.
DR OMA; YAADFKL; -.
DR PhylomeDB; Q57341; -.
DR BioCyc; HINF71421:G1GJ1-140-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 2.
DR Gene3D; 1.10.3720.10; -; 2.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 2.
DR SUPFAM; SSF161098; SSF161098; 2.
DR PROSITE; PS50928; ABC_TM1; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Iron; Iron transport;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..632
FT /note="Putative ferric transport system permease protein
FT FbpB 1"
FT /id="PRO_0000060017"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 140..345
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 431..632
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 632 AA; 70263 MW; 5EF460BEBCC14BC0 CRC64;
MGWASFNLTW AWFLPVIVYG ALPLLRLPQQ TQAKTELFLT ALSVLFMFIS ATVYKISMGY
SVIVLLVGYT ALATLSLAKL KVMQGDKFII ASLLCIILLI FFFIVYPTLA IFVSMFYDGD
TFAPQQVMRI LTQSYIVRVI TNSLFLSGFV GIVSTVFGLA FALYTTRIAR RTAFIGKIFS
ILPIVTPPFV VGLGVTLMLG RSGYVTEFLS TNFGFSSHNW LYGFNGIAIA QILAFAPISF
MILDGALKSV HPSIEEASYT LRANRYQTFY QIIFPLLRPA LANSFLIVFI QSLADFSNPL
VLGGSFDVIA TQIYFYIAGS QLDYASASTL GSMLLIFSLA IFIIQYIWIG NRSYVTVSGK
SYRGDVQELP NGLKYTIIGM LGFWVIFNMA LYGSIFYGSF TVNWGVNYTL TLKNYAMLFG
QGLSDGAWPS LINTLIYAGI AAPLTAFFGL LIAYIVVRKD FQGKKSLEFL TMLCFAVPGT
VAGVSYILAF NNAPLYITGT GIIVIISMVM RDLPIGMRAA IAGLGQLDKS LDEASLSLKG
SSWKTLCFIV LPLLKPALLS ALVTSFVRAM TTVSAIIFLV TADTRVYRIY FKSCGRRRIR
HCDCIRFYFN CCDDGNYFVF RLDCRRYAYF PF
