ID B2HFZ4_MYCMM Unreviewed; 451 AA.
AC B2HFZ4;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Conserved protein {ECO:0000313|EMBL:ACC41558.1};
GN OrderedLocusNames=MMAR_3123 {ECO:0000313|EMBL:ACC41558.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41558.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC41558.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP000854; ACC41558.1; -; Genomic_DNA.
DR RefSeq; WP_012394802.1; NC_010612.1.
DR AlphaFoldDB; B2HFZ4; -.
DR STRING; 216594.MMAR_3123; -.
DR GeneID; 34342739; -.
DR KEGG; mmi:MMAR_3123; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_11_2_11; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05675; M20_yscS_like; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 209..336
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 451 AA; 48815 MW; D5DFB463B5B9DAE5 CRC64;
MTQKNGETGT STDSRDDVAE VVSRLIRFDT TNTGEPETTK GEAECARWVA EQLAEVGYQT
EYVESGAPGR GNVFARLRGA DSSRGALLIH GHLDVVPAEA ADWSVHPFSG AIEDGYVWGR
GAVDMKDMVG MMIVVARHFR RAGIVPPRDL VFAFLADEEH GGHFGAHWLV DNRPDLFDGV
TEAVGEVGGF SLTVPRRDGG ERRLYLVETA EKGILWMRLT AQGRAGHGSM VHDHNAVTTV
AEAVARLGRH QFPLVITDTV AQFLHAVSEE TGLELDPGSP DLEGTLDKLG PIARMLKAVL
RDTANPTMLK AGYKANVIPA TAEAVVDCRV LPGRQAAFEA EVDELIGPDV SREWISELAS
YETSFDGDLV DAMNAAVLSV DPDGRTVPYM LSGGTDAKAF ARLGIRCFGF SPLRLPPELD
FAALFHGVDE RVPIDALRFG TEVLTHFLTH C
//
