ID A0A094PTD2_9ACTN Unreviewed; 697 AA.
AC A0A094PTD2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Beta-lactamase-related domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GM46_11825 {ECO:0000313|EMBL:KGA05286.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA05286.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA05286.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KGA05286.1}.
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DR EMBL; JNSG01000116; KGA05286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PTD2; -.
DR Proteomes; UP000029305; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..313
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT DOMAIN 424..628
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 697 AA; 78053 MW; 96FDEAC54F8609DE CRC64;
MTNEAVQEKL TTPQRDAALD GLRALAILRV ITWHASGWSW TTWIISSVPA MFVVTGALLA
RSLQKGSAFQ VLWKRFKRLL APLWCYSIVV YALSLYFQVR TSAIWTFFLP FNQPTSLIAS
QWFTSAMWYL RAYVWVLVLA PFIYALTRRW KSLIPAVGIV AVVAFGIWNT DTTGFSWAVG
DILLYSTCTA AGMAWLVHGR PSTRTLHYAA IAFLAGTCGW LLYRQPLDGV VNNDHVLHLF
VGGFWTALLL HFPNTLSSFS TTAVSRFLNK YPLSVYLWHS MAAWFFWQLV PKKIPTDIRI
LLIVGLTFAA LPAVTYLVGL FEHRKTGWFT LLQVLPRILL LAVILTSINV GPLSKKLDFV
RTPLNQPLPP SAAPKIVKID VEDDVKKFLD SSAFKDDTWS LRESEMQTIL DNRTKEMGLG
QTRAIVVTRD GRTWHGNSGN MKTFDQPSLI GSLTKTFTTT LIMQLVDEGL ISLDDPIGEL
GMGFKHGQIT IRQLLTHTSG LSKYKTKNGY VAKGTTPLDV LRYVSEQPLR NPPGSYVNYS
TSGFSLLGLV LEQKTGKTFE ELLRSRITDP LGYQISTFRG DYGSIGFSTG GMMMTMDDLA
DWTRRYFFDR TTTKEAWDWA MRDTTGMGAH GYCPCRNKTF LALGHIGGRT FASVDGDGTV
VIIDTTGILV LNNYKKTQTF AQELRLVAGG GKKYLYP
//
