ID   YHAM_ECOLI              Reviewed;         436 AA.
AC   P42626; P42627; Q2M998; Q6BF47;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 3.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=UPF0597 protein YhaM {ECO:0000255|HAMAP-Rule:MF_01845};
GN   Name=yhaM {ECO:0000255|HAMAP-Rule:MF_01845}; Synonyms=yhaN;
GN   OrderedLocusNames=b4470, JW5518;
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   SEQUENCE REVISION.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
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   POSSIBLE FUNCTION, INDUCTION BY CYSTEINE, OPERON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=27435271; DOI=10.1099/mic.0.000337;
RA   Shimada T., Tanaka K., Ishihama A.;
RT   "Transcription factor DecR (YbaO) controls detoxification of L-cysteine in
RT   Escherichia coli.";
RL   Microbiology 162:1698-1707(2016).
CC   -!- FUNCTION: Plays a role in L-cysteine detoxification; it has been
CC       speculated to be a cysteine desulfhydrase (PubMed:27435271).
CC       {ECO:0000303|PubMed:27435271}.
CC   -!- INDUCTION: Transcription induced by L-cysteine (in vivo), under control
CC       of DecR. Member of the dlsT(yhaO)-yhaM operon.
CC       {ECO:0000269|PubMed:16397293}.
CC   -!- DISRUPTION PHENOTYPE: Slightly increased sensitivity to excess L-
CC       cysteine, the effect is more pronounced in M9 minimal medium. Cells
CC       produce about 9% of wild-type levels of hydrogen sulfide in the
CC       presence of excess cysteine. {ECO:0000269|PubMed:27435271}.
CC   -!- SIMILARITY: Belongs to the UPF0597 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01845}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57912.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA57913.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57912.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U18997; AAA57913.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAT48167.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77158.1; -; Genomic_DNA.
DR   RefSeq; WP_000460499.1; NZ_LN832404.1.
DR   RefSeq; YP_026202.1; NC_000913.3.
DR   AlphaFoldDB; P42626; -.
DR   SMR; P42626; -.
DR   BioGRID; 4259262; 13.
DR   STRING; 511145.b4470; -.
DR   PaxDb; P42626; -.
DR   PRIDE; P42626; -.
DR   EnsemblBacteria; AAT48167; AAT48167; b4470.
DR   EnsemblBacteria; BAE77158; BAE77158; BAE77158.
DR   GeneID; 2847723; -.
DR   KEGG; ecj:JW5518; -.
DR   KEGG; eco:b4470; -.
DR   PATRIC; fig|511145.12.peg.3204; -.
DR   EchoBASE; EB2608; -.
DR   eggNOG; COG3681; Bacteria.
DR   HOGENOM; CLU_051840_0_0_6; -.
DR   InParanoid; P42626; -.
DR   OMA; GAMIPVM; -.
DR   PhylomeDB; P42626; -.
DR   BioCyc; EcoCyc:G7622-MON; -.
DR   BioCyc; MetaCyc:G7622-MON; -.
DR   PRO; PR:P42626; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
DR   GO; GO:0009093; P:cysteine catabolic process; IMP:UniProtKB.
DR   GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IMP:EcoCyc.
DR   GO; GO:1901367; P:response to L-cysteine; IEP:EcoCyc.
DR   HAMAP; MF_01845; UPF0597; 1.
DR   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR021144; UPF0597.
DR   PANTHER; PTHR30501; PTHR30501; 1.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   PIRSF; PIRSF006054; UCP006054; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..436
FT                   /note="UPF0597 protein YhaM"
FT                   /id="PRO_0000169448"
SQ   SEQUENCE   436 AA;  45361 MW;  3506FB665AAE2BBB CRC64;
     MFDSTLNPLW QRYILAVQEE VKPALGCTEP ISLALAAAVA AAELEGPVER VEAWVSPNLM
     KNGLGVTVPG TGMVGLPIAA ALGALGGNAN AGLEVLKDAT AQAIADAKAL LAAGKVSVKI
     QEPCDEILFS RAKVWNGEKW ACVTIVGGHT NIVHIETHDG VVFTQQACVA EGEQESPLTV
     LSRTTLAEIL KFVNEVPFAA IRFILDSAKL NCALSQEGLS GKWGLHIGAT LEKQCERGLL
     AKDLSSSIVI RTSAASDARM GGATLPAMSN SGSGNQGITA TMPVVVVAEH FGADDERLAR
     ALMLSHLSAI YIHNQLPRLS ALCAATTAAM GAAAGMAWLV DGRYETISMA ISSMIGDVSG
     MICDGASNSC AMKVSTSASA AWKAVLMALD DTAVTGNEGI VAHDVEQSIA NLCALASHSM
     QQTDRQIIEI MASKAR