ID F3Z114_DESAF Unreviewed; 670 AA.
AC F3Z114;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=Desaf_1576 {ECO:0000313|EMBL:EGJ49912.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49912.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49912.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49912.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP003221; EGJ49912.1; -; Genomic_DNA.
DR RefSeq; WP_014259689.1; NC_016629.1.
DR AlphaFoldDB; F3Z114; -.
DR STRING; 690850.Desaf_1576; -.
DR KEGG; daf:Desaf_1576; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic 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 Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..229
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 264..590
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 635..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 326
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 670 AA; 73636 MW; 34EF9FCA5A7ADAB4 CRC64;
MSVAYEPEGQ QPPRHGLILL QALIMALFCA FALRLWYLQV HKGEQFAQKA RENRLRQEFV
YAPRGLIYDR DGVLVAVNEP AYALGLIRED VADIEKTLAQ VSEWTGQDIA ELRAAYRQGR
KKVKPFDRII LAPNISFDLL SSIEAGSHRW PGLEIMVRPR RNYPQGPLLS QILGYVAEAN
DEEITRDPDL QLADTVGKQG LEYVLESQLR GRKGLRQMEV DASGRLLNER QVSQPSSGQS
VTMAIDLDLQ QFATEEMEKL GHAGAVVVME PFTGQVLAMV STPTFDNNAF ASGLSTEQWA
ALRDDPRHPL QNKATQGVYP PGSTFKLLVA LAGLHEGIID PSETVFCGGE MKLGRRVFRC
WNKHGHGRVD LKRGLVESCD VYFYEMGNRL GVDRMEAFAK ASGFGSTTGI DLPHEKGGLI
PSRNWKLQRF GERWQGGENL NFAIGQGYTL VSPLQLARFV SSLLNGGFLL KPLLVDSDEP
VVQGRLLASA QQIKMVLDTM VATVDMDRGT ARRLRRPDAR MGGKTGTAQV VKLKTEDRGK
KTEEIAYEFR DHAWLVSWGV KDGRAVVIVC LVEHGGHGGE AAGPVSRAIY DYLFGPLGGT
STTMDNWPYI AGVEPNPLDK YAIPLQIVPK TAAKAGKTGK SGKLAAPKSM TQPVGLVSAD
TTEGANSVSR
//
