ID   HMUV_BORAV              Reviewed;         261 AA.
AC   Q8L1U3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Hemin import ATP-binding protein HmuV {ECO:0000255|HAMAP-Rule:MF_01718};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01718};
GN   Name=hmuV {ECO:0000255|HAMAP-Rule:MF_01718}; Synonyms=bhuV;
OS   Bordetella avium.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN HEMIN TRANSPORT.
RC   STRAIN=4169;
RX   PubMed=12228263; DOI=10.1128/iai.70.10.5390-5403.2002;
RA   Murphy E.R., Sacco R.E., Dickenson A., Metzger D.J., Hu Y., Orndorff P.E.,
RA   Connell T.D.;
RT   "BhuR, a virulence-associated outer membrane protein of Bordetella avium,
RT   is required for the acquisition of iron from heme and hemoproteins.";
RL   Infect. Immun. 70:5390-5403(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin
CC       import. Responsible for energy coupling to the transport system
CC       (Probable). {ECO:0000305|PubMed:12228263}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HmuV),
CC       two transmembrane proteins (HmuU) and a solute-binding protein (HmuT).
CC       {ECO:0000255|HAMAP-Rule:MF_01718}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01718}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01718}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Heme (hemin)
CC       importer (TC 3.A.1.14.5) family. {ECO:0000255|HAMAP-Rule:MF_01718}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY095952; AAM28272.1; -; Genomic_DNA.
DR   RefSeq; WP_012418768.1; NZ_UFTG01000001.1.
DR   AlphaFoldDB; Q8L1U3; -.
DR   SMR; Q8L1U3; -.
DR   GeneID; 41394965; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51261; HMUV; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..261
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000269576"
FT   DOMAIN          3..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   261 AA;  28023 MW;  879C63E5D4175036 CRC64;
     MTLQAQDLSV DRGAKRILTQ VSLTLEPGRM LGLLGANGAG KSTLLACLSG ELEPVCGHIE
     INGKPLRSLA SAKQARLRAV LPQKPSLSFD LGVREVVGMG AYPYAELSPA DVDALCEKAL
     RQAGVSHLAG RRYLELSGGE QQRVQFARVL MQCQAAPAGQ PRYLMLDEPI SNLDPRHQID
     VLRTAHDLAR EAGVGVLVIV HDVNLSARWC DRLLLLAQGS VVADGAPAEV LTPANLRRVY
     GVEADVLPHP REAGTLLVLM R