ID S2X1L8_9ACTN Unreviewed; 650 AA.
AC S2X1L8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-lactamase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9306_00144 {ECO:0000313|EMBL:EPD33919.1};
OS Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionimicrobium.
OX NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD33919.1, ECO:0000313|Proteomes:UP000014417};
RN [1] {ECO:0000313|EMBL:EPD33919.1, ECO:0000313|Proteomes:UP000014417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD33919.1,
RC ECO:0000313|Proteomes:UP000014417};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:EPD33919.1}.
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DR EMBL; AGZR01000002; EPD33919.1; -; Genomic_DNA.
DR RefSeq; WP_016455005.1; NZ_KE150269.1.
DR AlphaFoldDB; S2X1L8; -.
DR STRING; 883161.HMPREF9306_00144; -.
DR HOGENOM; CLU_025328_0_0_11; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000014417; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000014417};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..650
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004502928"
FT DOMAIN 165..317
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 384..624
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 650 AA; 68162 MW; EAE06A298C01CC8A CRC64;
MAQKIFSRLA AAALACLFIA GCSKPGYTPP DGAEEIGEAL ANVLASGQFN GLQVAGDTQA
AEADFDEVIA GMQGLRPEVK VGEIKYEGTM ENPAAQVSLN QNYTFSRNVE PQDESASPEP
TPSISRWAFT SKANLVYEGG WKVSWAPSIV HPQLDEYTRL VYERTSPKRG IITDRNGAAI
VSEQPVYKVG VDKTKLNGAD GDESARRLAE LVKVDVDAYV SRFQASGPQA FVEALTVRSE
KLPEGIEEIP GAIALGANMP LAPSENFAGN IFGTVGEATA EEIKNSDGLL SAGDQVGKQG
LQKSADARLR GDTGHKISLK FRKSVSKQTQ EELAKPATPS AEPIVEADLF SLSPKGGEAV
QTTLNMSIQT KLEAALAKSP GKIAVAVLDK DGGILAAGTS PDVGSQPLAT VGQFPPGSTM
KVASSLALLR RGEKPTSKVD CSEKAEAGGR EFTNYPGYPK VFIGKISLAN ALAQSCNTAF
VNAKITSKEL SSAAASLGMG VDYDAGFDSF YGSVPATEDP VVAAANSFGQ GHVLVSPMAL
AAMSGSVNSG KSLVAHLRTD VVPTLDASPI TEDEAAQLKE MMEGVLKGTG SSYAKWLSGA
KTGTAEFEEG SETKTHIWVT GFSGDMSVAI IDYDAKDGKN FEPILTAIFK
//