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HMUV_METFK
ID   HMUV_METFK              Reviewed;         269 AA.
AC   Q1H0W2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Mfla_1607;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000284; ABE49875.1; -; Genomic_DNA.
DR   RefSeq; WP_011479829.1; NC_007947.1.
DR   AlphaFoldDB; Q1H0W2; -.
DR   SMR; Q1H0W2; -.
DR   STRING; 265072.Mfla_1607; -.
DR   EnsemblBacteria; ABE49875; ABE49875; Mfla_1607.
DR   KEGG; mfa:Mfla_1607; -.
DR   eggNOG; COG4559; Bacteria.
DR   HOGENOM; CLU_000604_1_11_4; -.
DR   OMA; DMHHQIN; -.
DR   OrthoDB; 1752365at2; -.
DR   Proteomes; UP000002440; 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; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..269
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000269601"
FT   DOMAIN          2..242
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   269 AA;  29363 MW;  6DCEBE9B93463B7C CRC64;
     MLEVIHTGLN IGSKTLLHDI SFIIKPGEMV AICGPNGAGK SSLIRLLCGE LKPSSGEVRW
     EGKSLAEWNL LQLARQRALM QQHAEVGFAY TALEIILLGR HPHHLGANRP QDYQIAMAAM
     QEVGAVHLAE QIYSTLSGGE QARVQMARVL AQIWESSQGA RLLLLDEPTA ALDPLQQHRM
     LTIARKWADK GDVAVVAIVH DLNLAAQYAD RIALLRDGRL QAIDRVESIM TPAMVEACFD
     LPCVLLNHPD GGTPMIAARR HPSSSMIAT
 
 
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