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Database: UniProt
Entry: F8EUA3_ZYMMT
LinkDB: F8EUA3_ZYMMT
Original site: F8EUA3_ZYMMT 
ID   F8EUA3_ZYMMT            Unreviewed;       410 AA.
AC   F8EUA3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Processing peptidase {ECO:0000313|EMBL:AEI38124.1};
DE            EC=3.4.24.64 {ECO:0000313|EMBL:AEI38124.1};
GN   OrderedLocusNames=Zymop_1230 {ECO:0000313|EMBL:AEI38124.1};
OS   Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS   10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI38124.1, ECO:0000313|Proteomes:UP000000491};
RN   [1] {ECO:0000313|EMBL:AEI38124.1, ECO:0000313|Proteomes:UP000000491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC   NCIMB 11200 / NRRL B-4491 / Barker I
RC   {ECO:0000313|Proteomes:UP000000491};
RX   PubMed=21742897; DOI=10.1128/JB.05273-11;
RA   Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA   Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT   "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT   lectotype strain ATCC 29192.";
RL   J. Bacteriol. 193:5049-5050(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CP002865; AEI38124.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8EUA3; -.
DR   STRING; 579138.Zymop_1230; -.
DR   KEGG; zmp:Zymop_1230; -.
DR   PATRIC; fig|579138.3.peg.1306; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_2_5; -.
DR   OMA; RYGWGEL; -.
DR   Proteomes; UP000000491; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AEI38124.1}.
FT   DOMAIN          22..163
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          170..340
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   410 AA;  44812 MW;  13F9769489710B6B CRC64;
     MQTLSPRLHR LGNGLAVAVE PMSGVETMAV GLYADVGARS EPAPYSGLAH MVEHMVFKGA
     GHRDARMIAE AAENCGGQLN AWTARDHTVY QARMLAEDWA LGLELVSDLV RAPILDAEEL
     VREKGVVLSE LGESHDTPDD IIHDHLQSVA FKNQALGRPV LGDEKSIAAI DRAALCHWVE
     DYYHPEGCVL AAAGKIDEDA FLKMAESRFG DWNKGHPLKI EKAHFIGGRY NDQRDSEQTH
     IALGFGGFAY HDPRSHALAL YASILGGGMS SRLFQRVREE QGLVYSIYSW TQAWVETGLL
     GIYCATDKED ADKALTLIRE IINHSLKTVT EEELQRAKAQ ARAGLLMGLE GVGPRCDHLA
     RQIQIHDRIV EPIEVASWIN SVSLEDILKV SQQALAGGEA LASVGDGLTL
//
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