ID   A6TM57_ALKMQ            Unreviewed;       589 AA.
AC   A6TM57;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:ABR47275.1};
GN   OrderedLocusNames=Amet_1063 {ECO:0000313|EMBL:ABR47275.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR47275.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP000724; ABR47275.1; -; Genomic_DNA.
DR   RefSeq; WP_012062317.1; NC_009633.1.
DR   AlphaFoldDB; A6TM57; -.
DR   STRING; 293826.Amet_1063; -.
DR   KEGG; amt:Amet_1063; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_3_1_9; -.
DR   OrthoDB; 9769691at2; -.
DR   Proteomes; UP000001572; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          115..174
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          195..576
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   589 AA;  67207 MW;  441FD3426ACF9C34 CRC64;
     MNLYWSLKEL YQSFEDEQFK RDLKQVDNFI ETMDQWSQTE LTTHEHAISK LEEGINQSQA
     LDHVFSKLYA FTVLTLSVDA KNNQAQQVLD SLQQKETKLT KSIVTFERWI GGLDNLSELI
     VSSDTLKEHH FFLSEIHDKN QYLLSDEEEI LISKMKNTGS KAWSKLQELL TSTLLIEINV
     DGETKKLPLP VVRNMSHDSD VSVRKSAFEA ELKAYGDIEE SSAAALNGIK GEVFTLSELR
     GYDSPLAETL IQNRMESNVL DTMLEAMRES LPSFQRYYRR KAALLGHQGG LPFYDLLAPM
     GSVNKKFSYE EARDYIVTNF RSFSDELADF AHHAFESQWI DAEPRQGKRG GAFCFNLHPI
     KESRILANFT GTFSDVTTLA HELGHAYHGY CLKDESILNS NYPMPIAETA SIFAESVVVN
     AALKEANDEE KLNLLEESIS SAGQVIVDIY SRYLFETAVF EKRRDYSLSV KEFKELMVSA
     QKEAYGDGLD HRVLHPYMWV NKPHYYSGSR SFYNFPYAFG LLFAKGLYAE YLIQGDAFIP
     KYNELLTATG KLPIIDVGKM VGIDVTSIEF WRNSLKLVER DIEQFIALS
//