ID A0A0D0WXD1_9ACTN Unreviewed; 657 AA.
AC A0A0D0WXD1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KIR63294.1};
GN ORFNames=TK50_20820 {ECO:0000313|EMBL:KIR63294.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR63294.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR63294.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR63294.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) 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:KIR63294.1}.
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DR EMBL; JXSX01000002; KIR63294.1; -; Genomic_DNA.
DR RefSeq; WP_043966112.1; NZ_JXSX01000002.1.
DR AlphaFoldDB; A0A0D0WXD1; -.
DR PATRIC; fig|47853.6.peg.4355; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000032254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR007887; MecA_N.
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; PF05223; MecA_N; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..657
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039442350"
FT DOMAIN 42..156
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 164..327
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 378..651
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 68654 MW; 00C1272C6A29A00F CRC64;
MHQTHPIRRG SARTRARRSL AALAATVLVA GTLVGCSSDD GPAPTVDAFL SGWGKGDLQA
VGFVTPAGLK VPAADVARQL RELSGELADT PPVLRRTGDP KVDANVATAG IRVAWALPGG
IRWEYDRQVR LTTGDDGQWR VIWEPQVVHE QLTDGDRIAL RRDAAPRAGV LDGAGKPIVT
PRPVVRVGLQ PSEVTDAKAV ARQLDAAFRA VRPAITPPVD LTDLPKRLAD ADPGAFVEVV
TLRDEAYRQI RSRIYDLPGT KFRAEKLDLA PTREFARAVL GSVDQAQADD LAAHPDRYRQ
GDLVGHGGLQ GRHDERLRGT PGLTVISERA GPDGTVAPTG TELFRQEPKP GQAVRTTLDV
ATQNAADAAL RGEKRRAALV AVRVGDGAVL AAANGPGAAG ENLAFTAQVP PGSTFKMVSA
LGLLDRGAVT LDGPVACPKT FTVDGRSFKN SDNFALGTVP FRTDFAKSCN TAFAALAPKL
GPDGLAETGR ALGLEAEWDL GLDAFTGKVS ADGSPAEQAA AAFGQGTTLV SPLAMAAATA
AVARGRWEQP KLVVDPAPAK AAPAGPQLKP ESVEPLRTMM REVVTAGTAT ALKDAPGGPV
HGKTGTAEYD DDPAHTHAWF VGWQGDVAFA VFVERGGSSG SSAVPIAERF LRALAAS
//
