UUP_CAUVC
ID UUP_CAUVC Reviewed; 608 AA.
AC Q45978;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP-binding protein Uup {ECO:0000255|HAMAP-Rule:MF_00848, ECO:0000303|PubMed:30597160};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00848};
DE AltName: Full=Holdfast attachment protein C {ECO:0000303|PubMed:8150261};
GN Name=uup {ECO:0000255|HAMAP-Rule:MF_00848, ECO:0000303|PubMed:30597160};
GN Synonyms=hfaC {ECO:0000303|PubMed:8150261}; OrderedLocusNames=CC_2631;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368, AND POSSIBLE FUNCTION.
RC STRAIN=CB2A;
RX PubMed=8150261; DOI=10.1111/j.1574-6968.1994.tb06697.x;
RA Kurtz H.D. Jr., Smit J.;
RT "The Caulobacter crescentus holdfast: identification of holdfast attachment
RT complex genes.";
RL FEMS Microbiol. Lett. 116:175-182(1994).
RN [3]
RP DISCUSSION OF SEQUENCE, AND FAMILY.
RX PubMed=30597160; DOI=10.1016/j.jmb.2018.12.013;
RA Murina V., Kasari M., Takada H., Hinnu M., Saha C.K., Grimshaw J.W.,
RA Seki T., Reith M., Putrins M., Tenson T., Strahl H., Hauryliuk V.,
RA Atkinson G.C.;
RT "ABCF ATPases involved in protein synthesis, ribosome assembly and
RT antibiotic resistance: structural and functional diversification across the
RT tree of life.";
RL J. Mol. Biol. 431:3568-3590(2019).
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:0000255|HAMAP-Rule:MF_00848}.
CC -!- FUNCTION: One of a cluster of genes involved in attachment of the
CC holdfast to the cell. The holdfast is a structure that allows the
CC bacteria to firmly adhere to surfaces. {ECO:0000303|PubMed:8150261}.
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:0000255|HAMAP-
CC Rule:MF_00848};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00848}.
CC Note=Associates with ribosomes. {ECO:0000255|HAMAP-Rule:MF_00848}.
CC -!- DOMAIN: The C-terminal domain (CTD) helps bind DNA.
CC {ECO:0000250|UniProtKB:P43672}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Uup subfamily. {ECO:0000255|HAMAP-Rule:MF_00848,
CC ECO:0000303|PubMed:30597160}.
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DR EMBL; AE005673; AAK24598.1; -; Genomic_DNA.
DR EMBL; U01165; AAA18638.1; -; Genomic_DNA.
DR PIR; B87575; B87575.
DR RefSeq; NP_421430.1; NC_002696.2.
DR RefSeq; WP_010920483.1; NC_002696.2.
DR AlphaFoldDB; Q45978; -.
DR SMR; Q45978; -.
DR STRING; 190650.CC_2631; -.
DR PRIDE; Q45978; -.
DR EnsemblBacteria; AAK24598; AAK24598; CC_2631.
DR KEGG; ccr:CC_2631; -.
DR PATRIC; fig|190650.5.peg.2643; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_5; -.
DR OMA; AQADKMR; -.
DR BioCyc; CAULO:CC2631-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00848; Uup; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032524; ABC_tran_C.
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 Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF16326; ABC_tran_CTD; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..608
FT /note="ATP-binding protein Uup"
FT /id="PRO_0000092340"
FT DOMAIN 7..217
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT DOMAIN 285..512
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT REGION 522..608
FT /note="C-terminal domain (CTD), binds DNA"
FT /evidence="ECO:0000250|UniProtKB:P43672"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT BINDING 317..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00848"
FT CONFLICT 36
FT /note="V -> E (in Ref. 2; AAA18638)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> D (in Ref. 2; AAA18638)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..368
FT /note="DF -> TS (in Ref. 2; AAA18638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 66006 MW; B067D2D373EE8B79 CRC64;
MASPARAPVL ALKDVRLADG AKPLFDGVDL ALEPRVRACL VGRNGAGKST LLKILAGQGV
EADSGERAVQ PGAKVVYVSQ EPEITGETLL DYATAGGAQD YEAQAALADF GLDPDKSAKG
LSGGETRRAA LARAFAEQPD VLLLDEPTNH LDIFAIQTLE DELAASKCAA LIVSHDRAFL
NRVTERCFWL EHRKIRRLDK GFSEFEAWAE SIMAADAEEA RRLDKVLERE NAWLARGVQG
RRARNEGRRR ALLALRAEKK DRQSELRGTM TMAVESAGTS GKRVVEAKGV TKRFGERTIV
ENFSTRILRG DRVALVGPNG AGKTTLVKLL LGELERDAGT VQLGTNLEVS YIDQARMALS
DKITVWDFLT PGGGDSIIVR GHPKHVAGYA KEFLFTDAQL RQPVTSLSGG ERNRLLLARA
LANPTNLMVL DEPTNDLDMD TLDLLEDLLA DFDGTLILVS HDRDFIDRLA SSTIALDGKG
GVVETPGGWT DLMDQNPDFF KASKGGTAFA PVSKAATKPA PAAPAAPKKS AKLSYKDQRR
LEECEALIAK SPAIIAKLEE ALADPNLYTR DPATFDKTMK ALDKARADLE QAEMEWLELE
EKKENLAG
