ID A0A3A9Z192_9ACTN Unreviewed; 652 AA.
AC A0A3A9Z192;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:RKN42018.1};
GN ORFNames=D7223_23000 {ECO:0000313|EMBL:RKN42018.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN42018.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN42018.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN42018.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
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:RKN42018.1}.
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DR EMBL; RBAK01000010; RKN42018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9Z192; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000281726; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000281726};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..652
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039716545"
FT DOMAIN 38..151
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 160..323
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 375..645
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 652 AA; 68561 MW; 94E96746B30D4CF7 CRC64;
MHLSYPRGRR RSHPALTLLT VTALVAGALT GCSSEDGPAK SVEAFLSGWR SGDLQAVGFV
DPTGAKVPAA DVAREIRELS GELAATPPAL RRVGDPKITR DTATATVAVE WTLPGGTRWA
YERPVRLKQA ADDAWQVIWE PAVVQEQLTR GDRLGLRRDT GPRAAVLDDD GQPLIAPRPV
IRVSLAPREV KDLPRLTRQL DAAFKAIRPA LVPPVDLSDL PKRVADADPE QLVEVVTLRE
DAYRQIKSRI YELPGTKFPG DTLDLAPTRE FARAALGTVD PAQADDLTRF PDRYVAGDLV
GHGGLQGRFD ERLRGAPGLT VIVERAGEDG KLVATGTELF RREPQPGQPV RTTLDVATQK
AADVALGGEK RRSALVAVRV SDGAVLAAAN GPGPAGENLA LTAQVPPGST FKMVSALALL
DKGAVTADAP VNCPKNYPVD GRSFKNSDDF ALGRVPFRTD FAKSCNTAFV ALAPQLGPDG
LAATGRTLGL EGQWDLGLDA FTGKVSANGG ATEQAAAAIG QGTTVVSPVA MAGATAAVAR
GRFVQPRLVL DPAPAKPAAD GPELAAESLT ALRAMMREVV TAGTATALAD VPGGPVHGKT
GTAEYDDDPR NTHAWFVGWQ GDVAFAVFVE KGGSSTSSAV PITERFLRAL PR
//
