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Database: UniProt
Entry: A3VMX1_9RHOB
LinkDB: A3VMX1_9RHOB
Original site: A3VMX1_9RHOB 
ID   A3VMX1_9RHOB            Unreviewed;       298 AA.
AC   A3VMX1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Putative Mrp (Multidrug resistance-associated proteins) family protein {ECO:0000313|EMBL:EAQ10400.1};
DE   Flags: Fragment;
GN   ORFNames=RB2654_21563 {ECO:0000313|EMBL:EAQ10400.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10400.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ10400.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10400.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC       binding proteins family. {ECO:0000256|ARBA:ARBA00008205}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MIP18 family.
CC       {ECO:0000256|ARBA:ARBA00007352}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ10400.1}.
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DR   EMBL; AAMT01000043; EAQ10400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3VMX1; -.
DR   STRING; 314271.RB2654_21563; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_0_5; -.
DR   Proteomes; UP000002931; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
DR   InterPro; IPR000808; Mrp-like_CS.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1.
DR   PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002931}.
FT   DOMAIN          6..77
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   REGION          83..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         298
FT                   /evidence="ECO:0000313|EMBL:EAQ10400.1"
SQ   SEQUENCE   298 AA;  30749 MW;  233A4E7053F494E4 CRC64;
     MMALTRDRVM SVLATVSMPD KGDLASRDMI RALTIDGGHV SFIIEAPSPE AAGAMEPQRK
     AAESAIAALD GVEKVTVILT AHGGTRPQPK KEAPNLRVGG HPTPQAGPQA IAGVKRVIAV
     ASGKGGVGKS TVSSNLAVAL AAAGRKVGLL DADILGPSQA LMMGVTEKPT SSDGKQLDPL
     VAHGVKVMSV GAIVDPDQAV VWRGPMLMGT LQQFAFQVNW GDLDVLIVDL PPGTGDVQLT
     LAQKVVMTGA LVVSTPQDVA LLDAHKAIDM FGKVSVPILG LIENMSSYVC PNCGHEAH
//
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