ID   HMUV_PSEAB              Reviewed;         255 AA.
AC   Q02FW7;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=PA14_62280;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01718}.
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; CP000438; ABJ14088.1; -; Genomic_DNA.
DR   RefSeq; WP_003095098.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02FW7; -.
DR   SMR; Q02FW7; -.
DR   PRIDE; Q02FW7; -.
DR   EnsemblBacteria; ABJ14088; ABJ14088; PA14_62280.
DR   KEGG; pau:PA14_62280; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; DMHHQIN; -.
DR   BioCyc; PAER208963:G1G74-5267-MON; -.
DR   Proteomes; UP000000653; Chromosome.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51261; HMUV; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..255
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000277703"
FT   DOMAIN          2..238
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   255 AA;  27525 MW;  F7CB956D8B205BA3 CRC64;
     MLRVENLSIR RGGKTVLEGL ELELRPGEML GVLGPNGAGK STLLGALCGE LEPAEGLVLL
     DERGLDDWPG VARAQRLAVL PQSSSLGFAF PVEAVVGFGR LPHSSGRERD VQIVAEALAA
     ADASHLAGRS YLALSGGERQ RVHLARVLAQ LWPGEPGQVL LLDEPTSALD PLHQHTTLQA
     VHDFARRGAS VLVILHDLNL AARYCDRLLL LQNGRPHLLG TPEEVLRPEP LRAVFGLEVL
     VQRHPERGHP LIVAR