ID   B0VU84_ACIBS            Unreviewed;       922 AA.
AC   B0VU84;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Protease {ECO:0000313|EMBL:CAP00422.1};
GN   OrderedLocusNames=ABSDF1071 {ECO:0000313|EMBL:CAP00422.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP00422.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP00422.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP00422.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CU468230; CAP00422.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VU84; -.
DR   KEGG; abm:ABSDF1071; -.
DR   HOGENOM; CLU_007487_1_1_6; -.
DR   BioCyc; ABAU509170:GCL9-864-MONOMER; -.
DR   Proteomes; UP000001741; 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:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CAP00422.1};
KW   Protease {ECO:0000313|EMBL:CAP00422.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..922
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002758108"
FT   DOMAIN          63..188
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..372
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          668..847
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   922 AA;  104216 MW;  699B6B815B5E6B40 CRC64;
     MFMQFKQLTL SLCIFGLSAA SFAQTTLVKS KQNVEEYKLD NGFRVVLAPN DKENKIFINT
     IYLTGSLNDP QGKSGLAHLL EHLAFKGTQN VKGEEFQRRL DQYTLMTNAS TDYYSTKYTN
     IVRPEKTALD QVLYLESERM DKLVLQEKFV PSEIEIVKRE REVRMDQPFA VLMDQMWKSA
     YGNQYLGRLP IGDLPELKSI KMPELNQFYR SWYAPNNAVM VISGKFDKTD VLKTIDQYFS
     PIPARAVPKP VQVPVLDSTK LKNREFVVKK GSDLAKFHIY MDGKNTKIQP ELAFAPMLYT
     MQPSGHLYQN MVETGVSTDV QASTWLDQDF NVVFLGAIYS PKNDPKKVES ALLSGIEKGK
     PFTETELNRV KSLMKTQGEL VNKDAVALGS RLSDYTVADG QWDQYFKDLD SIDKVKLNEV
     NQTLKQFLVA GHRIDGDILP TPEDQKKALQ LDAKDKPKTL DQTDVKAEPL KDPKVYQQEV
     AEFLKTSKQY AESNEKKIIR GKLKNGMKYA LFPVETRDDR TYATITMDFG TEKSLFDKGT
     VVDLTSYLLL RGSDKYSLQD IADKSIDAGG AAYASTDGNG NGMTINIQSK TEKFDEFFKF
     VLEVMKNPKF EQSQFDLIKS QSLSSLDRPY TEPDVVAGLT LSRLIEEYQP GDLRYHFEPE
     LAKKQLKNVT QEQVKELYQH FFAMSHAQIA ITGAFDAKKM KKLLNQEFGS WNSKQPYEKI
     LIQHVDFPAQ QVHALSEQRE FGSYQSVLAL PVGKKHPDAS ALILMNYILG ESQISSRLAQ
     ELREKNALVY GFGTGLQLDR DTNVGALSIS ANYTAGRSAQ VSASVHKVLN DLITQGITEQ
     ELAAAKADIM KKRVTALEDE RNIHGMLNLE LESGKTLLDR VKHDQELTKL TVADVNTVIK
     KYIKPSNLVE VMADQYGQAQ KQ
//