RCLA_ECOLI
ID RCLA_ECOLI Reviewed; 441 AA.
AC P77212; Q2MCB8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable pyridine nucleotide-disulfide oxidoreductase RclA;
DE AltName: Full=Reactive chlorine resistance protein A;
GN Name=rclA; Synonyms=ykgC; OrderedLocusNames=b0304, JW5040;
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;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24078635; DOI=10.1074/jbc.m113.503516;
RA Parker B.W., Schwessinger E.A., Jakob U., Gray M.J.;
RT "The RclR protein is a reactive chlorine-specific transcription factor in
RT Escherichia coli.";
RL J. Biol. Chem. 288:32574-32584(2013).
CC -!- FUNCTION: Probably involved in reactive chlorine species (RCS) stress
CC resistance. {ECO:0000269|PubMed:24078635}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- INDUCTION: Induced by RclR in response to hypochlorous acid (HOCl).
CC {ECO:0000269|PubMed:24078635}.
CC -!- DISRUPTION PHENOTYPE: Mutants are more sensitive to HOCl treatment than
CC wild-type cells. {ECO:0000269|PubMed:24078635}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18031.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73857; AAB18031.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73407.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76088.1; -; Genomic_DNA.
DR PIR; H64756; H64756.
DR RefSeq; NP_414838.2; NC_000913.3.
DR RefSeq; WP_001046307.1; NZ_SSUW01000013.1.
DR PDB; 6KGY; X-ray; 2.90 A; A/B/C/D=1-441.
DR PDB; 6KOD; X-ray; 3.00 A; A/B/C/D=1-441.
DR PDB; 6KYY; X-ray; 2.80 A; A/B/C/D=1-441.
DR PDBsum; 6KGY; -.
DR PDBsum; 6KOD; -.
DR PDBsum; 6KYY; -.
DR AlphaFoldDB; P77212; -.
DR SMR; P77212; -.
DR BioGRID; 4259800; 12.
DR DIP; DIP-12675N; -.
DR IntAct; P77212; 2.
DR STRING; 511145.b0304; -.
DR jPOST; P77212; -.
DR PaxDb; P77212; -.
DR PRIDE; P77212; -.
DR EnsemblBacteria; AAC73407; AAC73407; b0304.
DR EnsemblBacteria; BAE76088; BAE76088; BAE76088.
DR GeneID; 946092; -.
DR KEGG; ecj:JW5040; -.
DR KEGG; eco:b0304; -.
DR PATRIC; fig|511145.12.peg.311; -.
DR EchoBASE; EB3350; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_2_6; -.
DR InParanoid; P77212; -.
DR OMA; RIAAYAM; -.
DR PhylomeDB; P77212; -.
DR BioCyc; EcoCyc:G6174-MON; -.
DR BioCyc; MetaCyc:G6174-MON; -.
DR PRO; PR:P77212; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008823; F:cupric reductase activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:EcoCyc.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:1901530; P:response to hypochlorite; IMP:EcoCyc.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome; Stress response.
FT CHAIN 1..441
FT /note="Probable pyridine nucleotide-disulfide
FT oxidoreductase RclA"
FT /id="PRO_0000068059"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 33..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:6KYY"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6KYY"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6KYY"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6KGY"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 366..370
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:6KYY"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6KYY"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 432..436
FT /evidence="ECO:0007829|PDB:6KYY"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:6KGY"
SQ SEQUENCE 441 AA; 48244 MW; 53B9C0B52C7DA8A0 CRC64;
MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP TKTLVHDAQQ
HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVIDGQAE FINNHSLRVH RPEGNLEIHG
EKIFINTGAQ TVVPPIPGIT TTPGVYDSTG LLNLKELPGH LGILGGGYIG VEFASMFANF
GSKVTILEAA SLFLPREDRD IADNIATILR DQGVDIILNA HVERISHHEN QVQVHSEHAQ
LAVDALLIAS GRQPATASLH PENAGIAVNE RGAIVVDKRL HTTADNIWAM GDVTGGLQFT
YISLDDYRIV RDELLGEGKR STDDRKNVPY SVFMTPPLSR VGMTEEQARE SGADIQVVTL
PVAAIPRARV MNDTRGVLKA IVDNKTQRML GASLLCVDSH EMINIVKMVM DAGLPYSILR
DQIFTHPSMS ESLNDLFSLV K
