YBHC_ECOLI
ID YBHC_ECOLI Reviewed; 427 AA.
AC P46130; P75765;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Putative acyl-CoA thioester hydrolase YbhC;
DE EC=3.1.2.-;
DE Flags: Precursor;
GN Name=ybhC; OrderedLocusNames=b0772, JW0755;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 33-427.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-300.
RC STRAIN=K12;
RA Taylor A., Smith G.R., Gardner J.F.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=331474; DOI=10.1126/science.331474;
RA Landy A., Ross W.;
RT "Viral integration and excision: structure of the lambda att sites.";
RL Science 197:1147-1160(1977).
RN [6]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10806384; DOI=10.1046/j.1432-1327.2000.01296.x;
RA Molloy M.P., Herbert B.R., Slade M.B., Rabilloud T., Nouwens A.S.,
RA Williams K.L., Gooley A.A.;
RT "Proteomic analysis of the Escherichia coli outer membrane.";
RL Eur. J. Biochem. 267:2871-2881(2000).
RN [8]
RP FUNCTION.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 29-427, ABSENCE OF PECTINASE
RP ACTIVITY, ABSENCE OF PECTIN BINDING, ABSENCE OF ACYL COENZYME A ESTERASE
RP ACTIVITY, DISULFIDE BOND, AND FUNCTION.
RX PubMed=19452549; DOI=10.1002/prot.22453;
RA Ekloef J.M., Tan T.-C., Divne C., Brumer H.;
RT "The crystal structure of the outer membrane lipoprotein YbhC from
RT Escherichia coli sheds new light on the phylogeny of carbohydrate esterase
RT family 8.";
RL Proteins 76:1029-1036(2009).
CC -!- FUNCTION: Putative thioesterase. Does not bind pectin, and has no
CC pectinesterase activity. {ECO:0000269|PubMed:15808744,
CC ECO:0000269|PubMed:19452549}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Asp residue in position 252 essential for
CC pectinase activity. Likewise, most of the residues involved in
CC substrate binding are not conserved. Was originally (PubMed:15808744)
CC thought to have palmitoyl-CoA thioesterase activity, but
CC PubMed:19452549 were unable to detect any pectinase or palmitoyl-CoA
CC thioesterase activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305|PubMed:15808744}.
CC -!- SEQUENCE CAUTION:
CC Sequence=U39938; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC73859.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35436.2; -; Genomic_DNA.
DR EMBL; U39938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D64813; D64813.
DR RefSeq; NP_415293.1; NC_000913.3.
DR RefSeq; WP_001091569.1; NZ_STEB01000028.1.
DR PDB; 3GRH; X-ray; 1.70 A; A=29-427.
DR PDBsum; 3GRH; -.
DR AlphaFoldDB; P46130; -.
DR SMR; P46130; -.
DR BioGRID; 4261839; 24.
DR DIP; DIP-11407N; -.
DR IntAct; P46130; 3.
DR STRING; 511145.b0772; -.
DR jPOST; P46130; -.
DR PaxDb; P46130; -.
DR PRIDE; P46130; -.
DR EnsemblBacteria; AAC73859; AAC73859; b0772.
DR EnsemblBacteria; BAA35436; BAA35436; BAA35436.
DR GeneID; 66670957; -.
DR GeneID; 945381; -.
DR KEGG; ecj:JW0755; -.
DR KEGG; eco:b0772; -.
DR PATRIC; fig|1411691.4.peg.1506; -.
DR EchoBASE; EB2713; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_5_0_6; -.
DR InParanoid; P46130; -.
DR OMA; FNRMWEY; -.
DR PhylomeDB; P46130; -.
DR BioCyc; EcoCyc:EG12875-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR EvolutionaryTrace; P46130; -.
DR PRO; PR:P46130; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl esterase; Cell outer membrane; Disulfide bond;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..427
FT /note="Putative acyl-CoA thioester hydrolase YbhC"
FT /id="PRO_0000023502"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT DISULFID 185..197
FT /evidence="ECO:0000269|PubMed:19452549"
FT CONFLICT 167
FT /note="N -> Q (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 279..297
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3GRH"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3GRH"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:3GRH"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3GRH"
SQ SEQUENCE 427 AA; 46082 MW; 208831BE0EDBCB5C CRC64;
MNTFSVSRLA LALAFGVTLT ACSSTPPDQR PSDQTAPGTS SRPILSAKEA QNFDAQHYFA
SLTPGAAAWN PSPITLPAQP DFVVGPAGTQ GVTHTTIQAA VDAAIIKRTN KRQYIAVMPG
EYQGTVYVPA APGGITLYGT GEKPIDVKIG LSLDGGMSPA DWRHDVNPRG KYMPGKPAWY
MYDSCQSKRS DSIGVLCSAV FWSQNNGLQL QNLTIENTLG DSVDAGNHPA VALRTDGDQV
QINNVNILGR QNTFFVTNSG VQNRLETNRQ PRTLVTNSYI EGDVDIVSGR GAVVFDNTEF
RVVNSRTQQE AYVFAPATLS NIYYGFLAVN SRFNAFGDGV AQLGRSLDVD ANTNGQVVIR
DSAINEGFNT AKPWADAVIS NRPFAGNTGS VDDNDEIQRN LNDTNYNRMW EYNNRGVGSK
VVAEAKK
