PBPAD_CLOAB
ID PBPAD_CLOAB Reviewed; 434 AA.
AC Q97H19;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Putative polysaccharide biosynthesis protein with aminopeptidase-like domain;
GN OrderedLocusNames=CA_C2195;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH ZINC, SUBUNIT, AND
RP PUTATIVE FUNCTION.
RX PubMed=24646163; DOI=10.1186/1471-2105-15-75;
RA Das D., Murzin A.G., Rawlings N.D., Finn R.D., Coggill P., Bateman A.,
RA Godzik A., Aravind L.;
RT "Structure and computational analysis of a novel protein with
RT metallopeptidase-like and circularly permuted winged-helix-turn-helix
RT domains reveals a possible role in modified polysaccharide biosynthesis.";
RL BMC Bioinformatics 15:75-75(2014).
CC -!- FUNCTION: The genomic context suggests a role in the biosynthesis of
CC modified polysaccharides; this association with genes involved in
CC carbohydrate metabolism is observed in several phylogenetically
CC distinct taxa. Is not expected to have peptidase activity despite low
CC similarity to aminopeptidases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24646163}.
CC -!- DOMAIN: Contains an N-terminal region with low similarity to
CC aminopeptidases, an insert domain, and a C-terminal permutated winged
CC helix-turn-helix domain.
CC -!- SIMILARITY: Belongs to the UPF0770 family. {ECO:0000305}.
CC -!- CAUTION: Has distant sequence similarity to aminopeptidases that belong
CC to the MEROPS peptidase family M28, but binds only one zinc ion,
CC contrary to the metallopeptidases of the MEROPS family M28 that bind
CC two catalytic zinc ions. Lacks the active site Asp and Glu residues
CC that are conserved in family members with aminopeptidase activity.
CC {ECO:0000305}.
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DR EMBL; AE001437; AAK80152.1; -; Genomic_DNA.
DR PIR; E97170; E97170.
DR RefSeq; NP_348812.1; NC_003030.1.
DR RefSeq; WP_010965493.1; NC_003030.1.
DR PDB; 3K9T; X-ray; 2.37 A; A=1-434.
DR PDBsum; 3K9T; -.
DR AlphaFoldDB; Q97H19; -.
DR SMR; Q97H19; -.
DR STRING; 272562.CA_C2195; -.
DR EnsemblBacteria; AAK80152; AAK80152; CA_C2195.
DR GeneID; 44998674; -.
DR KEGG; cac:CA_C2195; -.
DR PATRIC; fig|272562.8.peg.2396; -.
DR eggNOG; COG4310; Bacteria.
DR HOGENOM; CLU_052015_0_0_9; -.
DR OMA; TVPQEWN; -.
DR OrthoDB; 1533953at2; -.
DR EvolutionaryTrace; Q97H19; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR032610; DUF2172.
DR InterPro; IPR032589; DUF4910.
DR InterPro; IPR012353; UCP015244.
DR InterPro; IPR032622; UCP01524_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF09940; DUF2172; 1.
DR Pfam; PF16254; DUF4910; 1.
DR Pfam; PF16221; HTH_47; 1.
DR PIRSF; PIRSF015244; UCP015244; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..434
FT /note="Putative polysaccharide biosynthesis protein with
FT aminopeptidase-like domain"
FT /id="PRO_0000429355"
FT REGION 1..55
FT /note="Aminopeptidase-like"
FT REGION 56..164
FT /note="Insert"
FT REGION 57..355
FT /note="Aminopeptidase-like"
FT REGION 356..434
FT /note="Permutated winged helix-turn-helix"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24646163"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24646163"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24646163"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3K9T"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3K9T"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 150..163
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3K9T"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:3K9T"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3K9T"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 404..411
FT /evidence="ECO:0007829|PDB:3K9T"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:3K9T"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3K9T"
SQ SEQUENCE 434 AA; 49870 MW; A14113706360C85E CRC64;
MEEINKYIQN SSETGGEIYN LIEELFPICR SITGNGVRKT MDIIRKHIPL EIHEVKSGTK
VFDWTVPKEW NIKDAYVRNS KGEKVIDFKE NNLHVMSYSV PVHKTMTLDE LKPYLHTIPG
NKDRIPYLTS YYKENWGFSL TQNKFDELCD DDYEVVIDSS LEDGSLTYGE YYIRGELEEE
ILLTTYTCHP SMCNDNLSGV ALITFIAKAL SKLKTKYSYR FLFAPETIGS ITWLSRNEDK
LKNIKMGLVA TCVGDAGIKN YKRTKFGDAE IDKIVEKVLM HCGSEYYVAD FFPWGSDERQ
FSSPGINLPV GSLMRSCYGF DGYHTSADNL CYMNKDGLAD SYKTYLEVIY TIENNRTYLN
LNPKCEPQLG KRGIYRMIGG GSDYPFDEFA MFWVLNMSDG KNSLLDIAYK SGMEFRRIKY
AADALYRVEL LKLV
