ID   F0KMW4_ACICP            Unreviewed;       677 AA.
AC   F0KMW4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Metallopeptidase {ECO:0000313|EMBL:ADY81566.1};
GN   Name=thoP1 {ECO:0000313|EMBL:ADY81566.1};
GN   OrderedLocusNames=BDGL_000980 {ECO:0000313|EMBL:ADY81566.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY81566.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY81566.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY81566.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
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|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP002177; ADY81566.1; -; Genomic_DNA.
DR   RefSeq; WP_014206614.1; NC_016603.1.
DR   RefSeq; YP_004995248.1; NC_016603.1.
DR   AlphaFoldDB; F0KMW4; -.
DR   STRING; 871585.BDGL_000980; -.
DR   GeneID; 11639161; -.
DR   KEGG; acc:BDGL_000980; -.
DR   PATRIC; fig|871585.3.peg.979; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_2_1_6; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000007477; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06455; M3A_TOP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..677
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003255960"
FT   DOMAIN          236..670
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   677 AA;  77691 MW;  36EA4026CF481C70 CRC64;
     MKKIGDTMKN NALKMTTLCM LTIGVSQFAM AETTRPTLPL LKAQQLPAWC DANLKKIQKE
     ISNFEKTPVK DNAAAAPILA KWDKVFAHFE DFSGPISLYS NVDPDAKLRK AAEDCEIKIN
     QFHTDIFQNS KLYNVIKNTK ATDPIDQKYR QDILDQFEDT GVQLEPVKRA RMKAILDELT
     KLEQEYARNV RDNPEKLEFT PEEMKGLPQS YISALKKNAK GKYLLGFEYP EYRPFMELAD
     NDDARKRYQI AFTRRGTEQN LKLLKQAIDL RYELAQLFGK ASYADWVLKD RMAKTPEAVN
     QFLAEVQKTV APLERKEVEE LREFKAQTLK TPLEKTEITR WSEAYWSEKL RKSKYQIDQE
     KLRDYFPTLA AQKWLFAISS DLYGIDFKPV KVKAWQDEVE YYDVVDKKTG KLLGGLYMDK
     FPREGKYGHA AVWGVYGGST LTNRLPVSAL VTNFNRKGLN SDELETFVHE FGHALHGILS
     NTRYTSQSGT SVERDFVEAP SQMYEEWARR KETLSKVADY CDPACPRVDD ELIARLKAVH
     NYGRGLRYAR QTLYAQYDMS LHTADALKVK PLENWQKMEA ATALGYVPTT EFPGQFGHLM
     GGYQAGYYGY MWSEVLALDM LSAYGDNLNN PQVGQRYRQT ILSQGSQKPA AELVKDFLGR
     DPDNKAFFNE ITGQRVK
//