ID   N9R9U6_9GAMM            Unreviewed;       394 AA.
AC   N9R9U6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN   ORFNames=F889_00606 {ECO:0000313|EMBL:ENX35907.1};
OS   Acinetobacter colistiniresistens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=280145 {ECO:0000313|EMBL:ENX35907.1, ECO:0000313|Proteomes:UP000013009};
RN   [1] {ECO:0000313|EMBL:ENX35907.1, ECO:0000313|Proteomes:UP000013009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 1859 {ECO:0000313|EMBL:ENX35907.1,
RC   ECO:0000313|Proteomes:UP000013009};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. NIPH 1859.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENX35907.1}.
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DR   EMBL; APRZ01000007; ENX35907.1; -; Genomic_DNA.
DR   AlphaFoldDB; N9R9U6; -.
DR   PATRIC; fig|1217695.3.peg.583; -.
DR   HOGENOM; CLU_020027_10_0_6; -.
DR   Proteomes; UP000013009; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..394
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004152085"
FT   DOMAIN          40..384
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   394 AA;  43515 MW;  7910E1E4E37A3AB4 CRC64;
     MNLNDISRTS KQLLFMTGLV CASPMLWAQP LNEQQVKAIV DQQFKPLLAQ YNIPGMAVAV
     TLNGQHYFIN YGLASKQSQQ AVSNNTLFEL GSVSKTFNAT LASYAQAQGQ LSLSDHPAKY
     FPELKNTAVD RATLLNLGTY TAGGFPLQFP DQVVQQQDMI KYFQTWQAKT KVGAARQYSN
     PSIGLMGYVT ARAMKKPYAE LLEKTLFPQL GLTQSFIQVP EQQMPQYAWG YKADQALRVS
     PGMLDAEAYG VKSSSADMLR FLDVQINPQH LKQPLRKAIE NTHVGYFKVG AMTQGLGWEQ
     YAYPVKLETL LQGNSSKMAL ESHPAIAIKR PKIAPAATYF NKTGSSNGFG AYAAFIPEQK
     IGIVMLANTN FPNEARIQAS YTVVQQLLQA NTAQ
//