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Database: UniProt
Entry: A0A161RCH6_9NEIS
LinkDB: A0A161RCH6_9NEIS
Original site: A0A161RCH6_9NEIS 
ID   A0A161RCH6_9NEIS        Unreviewed;       636 AA.
AC   A0A161RCH6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ATP-binding protein Uup {ECO:0000256|HAMAP-Rule:MF_00848};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00848};
GN   Name=uup {ECO:0000256|HAMAP-Rule:MF_00848};
GN   ORFNames=AVW16_05665 {ECO:0000313|EMBL:KZE34968.1};
OS   Crenobacter luteus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Crenobacter.
OX   NCBI_TaxID=1452487 {ECO:0000313|EMBL:KZE34968.1, ECO:0000313|Proteomes:UP000076625};
RN   [1] {ECO:0000313|Proteomes:UP000076625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN10 {ECO:0000313|Proteomes:UP000076625};
RA   Hong K.W.;
RT   "Draft genome of Chromobacterium sp. F49.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably plays a role in ribosome assembly or function. May
CC       be involved in resolution of branched DNA intermediates that result
CC       from template switching in postreplication gaps. Binds DNA and has
CC       ATPase activity. {ECO:0000256|HAMAP-Rule:MF_00848}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00848};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00848}.
CC       Note=Associates with ribosomes. {ECO:0000256|HAMAP-Rule:MF_00848}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       Uup subfamily. {ECO:0000256|HAMAP-Rule:MF_00848}.
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:KZE34968.1}.
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DR   EMBL; LQQU01000004; KZE34968.1; -; Genomic_DNA.
DR   RefSeq; WP_066609840.1; NZ_LQQU01000004.1.
DR   AlphaFoldDB; A0A161RCH6; -.
DR   STRING; 1452487.AVW16_05665; -.
DR   OrthoDB; 9762051at2; -.
DR   Proteomes; UP000076625; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   HAMAP; MF_00848; Uup; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032524; ABC_tran_C.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR043686; Uup.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR   PANTHER; PTHR42855:SF1; ABC TRANSPORTER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF16326; ABC_tran_CTD; 1.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00848}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00848};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00848};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00848};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00848};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00848};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00848}; Reference proteome {ECO:0000313|Proteomes:UP000076625};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00848}.
FT   DOMAIN          1..255
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          322..540
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          539..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
FT   BINDING         354..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00848"
SQ   SEQUENCE   636 AA;  70810 MW;  09E8DE3FF890F91F CRC64;
     MALLTVEKAA LAFGHVPLLD NVDFALEPGE VVGLIGRNGA GKSSLLKAIA GAVKLDDGRV
     VARNDVKIAY VPQEPVFDLE HTVFEAVAEG LGDVKALLTD YHKATQRLAE PGADHEAALA
     DIERLQHALE AANGWQFDAL IAATLSHLGL DADVRVGELS GGWKKRVALA RALAAKPDIL
     LLDEPTNHLD VAAIEWLESL LKAFAGSVLL ITHDRRFLDN VATRIVELDR GVLRSYPGSF
     SAYQTRKAEE LAIEEEQNRV FDKFHAQEEA WIRKGIEARR TRNEGRVRRL EQIRRERAAR
     RERVGQVNFQ LDPGERSGKL VAELEHVGKG YEGKTLIRDF TSRILRGDKI GLIGPNGAGK
     TTLLKLILGE LEPDSGTVKR GTKLEIAYFD QFREQLDEEM SVADVISQGN DFVEIGGQKK
     HVMSYLEDFL FDPARARSPV KSLSGGERNR LLLARLFTRP ANVLVLDEPT NDLDIDTLEL
     LEEVLGQYSG TVFLVSHDRA FLDNVVTQVI AFEGDGQLNE YPGGYQDWVD ARARMAAMKP
     AEKKKEAPSA NVEKPAREKP KSNKLSFNEK RELERLPDEI AALEAEQAQL TEKLIDPNAY
     RDTPQEARGW QARIDQIDEL LLDKLARWEE LEAKTQ
//
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