ID   A9BAT6_PROM4            Unreviewed;       417 AA.
AC   A9BAT6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Possible Zn-dependent peptidase {ECO:0000313|EMBL:ABX08948.1};
GN   OrderedLocusNames=P9211_10171 {ECO:0000313|EMBL:ABX08948.1};
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08948.1, ECO:0000313|Proteomes:UP000000788};
RN   [1] {ECO:0000313|EMBL:ABX08948.1, ECO:0000313|Proteomes:UP000000788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP000878; ABX08948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9BAT6; -.
DR   STRING; 93059.P9211_10171; -.
DR   KEGG; pmj:P9211_10171; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_2_3; -.
DR   Proteomes; UP000000788; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000788}.
FT   DOMAIN          24..162
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..347
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   417 AA;  46452 MW;  66FA0C438B7E4DBB CRC64;
     MQDLKINRLA LRSGAECIST SMPESALTCI DLWCKAGSSF EDSDEKGMAH FLEHMIFKGS
     SKLREGEFDL KIEALGGSSN AATGFDDVHF YVLVPSEGVE QAIKLLIELV LCPSIMKNAY
     SLEREVVLEE IAQQSDQPDE KVFQMVLEGC WSNHPYGKSI LGNASSLNAS TPNRMKLFHQ
     RLYKPENCVL SIAGKSPRNL LKILSEGELG KQVDKSNPNN SKPNSKKLNF NIGRKIVEVK
     RLESARLVMA WPVPPASEQF IIMGYDIATT LLGEGRRSRL VNNLREEQQI VESIEMDLTA
     LEQGGLVLLE ACCIEKNLNK VEDSINQILI ESINSPPSER ETKRAKELVR NGFCFSLEHP
     AQVAAITGTQ TLWNRHQPLL EPLKDIDGWS SSMIQEEIFS CLQPSQCFTL IAKPLSS
//