ID A0A2T5P3M0_9NEIS Unreviewed; 688 AA. AC A0A2T5P3M0; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 05-DEC-2018, entry version 5. DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:PTU72333.1}; GN ORFNames=DBB33_00305 {ECO:0000313|EMBL:PTU72333.1}; OS Chromobacterium haemolyticum. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=394935 {ECO:0000313|EMBL:PTU72333.1, ECO:0000313|Proteomes:UP000244230}; RN [1] {ECO:0000313|EMBL:PTU72333.1, ECO:0000313|Proteomes:UP000244230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-11053 {ECO:0000313|EMBL:PTU72333.1, RC ECO:0000313|Proteomes:UP000244230}; RX PubMed=29670144; DOI=.1038/s41598-018-24296-0; RA Saraiva R.G., Huitt-Roehl C.R., Tripathi A., Cheng Y.-Q., Bosch J., RA Townsend C.A., Dimopoulos G.; RT "Chromobacterium spp. mediate their anti-Plasmodium activity through RT secretion of the histone deacetylase inhibitor romidepsin."; RL Sci. Rep. 8:6176-6176(2018). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PTU72333.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QARW01000002; PTU72333.1; -; Genomic_DNA. DR Proteomes; UP000244230; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR InterPro; IPR001193; MBTPS2. DR InterPro; IPR039562; MFP_biotin_lipoyl_2. DR PANTHER; PTHR13325; PTHR13325; 1. DR Pfam; PF13533; Biotin_lipoyl_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000244230}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 259 279 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 335 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 383 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 404 420 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 440 478 Biotin_lipoyl_2. {ECO:0000259|Pfam: FT PF13533}. SQ SEQUENCE 688 AA; 76498 MW; 8C0CB56EC4F7E09F CRC64; MHPGPVLADG APSWTLHDPC AHRFYQLGWA SFEILSRWRL GTAEAVLQAV NAETTLQLGA EDIEAVLLFL SRHQLLQAAS VEQNGWLWQL REANRPSRAM WLLKNYLFFR VPLLRPEALL NRLLPWTGWL FHPRFWLAMG AVLLLALALV SRRWDEFTHT FSAYGGVSAA IGIGVSLSLA KILHEMGHAL TARHFGCRVP AMGVAFLVMM PVLYTDTNDA WKLNSRRQRL LIGGAGMLAE LVLAAWATLL WSFLPDGPLR AGVFLLATTT WLATLAINAS PFMRFDGYFL LADYLGLPNL HNRAFALARW QLRKTLLGLD DPVPEHFPAA RRRGLILFAW ATWLYRLVLF LSIAFLVYHL FFKALGMLLL AVELGWFIAR PVVGELMVWW QRRTDLRWGR ATRRSAAALL VLTLALILPW QREVASPAVL GALQSQGLYA PAAGEVAEVL VRDGQLVKAG QIMARLSSPM LEAQLALAGA RERDLAWQTA QQPFDLELQQ RGPALRKQWQ VAQEQVAALR QQMARLTLAA PFSGRVVDVS DALRAGTALA EGEHLLDVVG SDGVKGEAFV EEAALNGLKP GHVARFVADG GEFWSVECRL GQIDRLNLPL LDQPLLASTY GGPVPTEQRD RGLVPLAATF RVRLERCDRS GAPLRELAGV ARLQGERYSL LERGLRQLLA VFRREAGL //