ID A0A0N1K991_9ACTN Unreviewed; 739 AA.
AC A0A0N1K991;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KPC84885.1};
GN ORFNames=ADK82_02325 {ECO:0000313|EMBL:KPC84885.1};
OS Streptomyces sp. NRRL S-4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519471 {ECO:0000313|EMBL:KPC84885.1, ECO:0000313|Proteomes:UP000037987};
RN [1] {ECO:0000313|Proteomes:UP000037987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-4 {ECO:0000313|Proteomes:UP000037987};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KPC84885.1}.
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DR EMBL; LGKJ01000001; KPC84885.1; -; Genomic_DNA.
DR RefSeq; WP_053928594.1; NZ_LGKJ01000001.1.
DR AlphaFoldDB; A0A0N1K991; -.
DR STRING; 1519471.ADK82_02325; -.
DR PATRIC; fig|1519471.3.peg.479; -.
DR Proteomes; UP000037987; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0009252; P:peptidoglycan biosynthetic process; 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 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 60..246
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 298..658
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 682..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 80057 MW; 01521ADAEB8B61B7 CRC64;
MSNIPETGRT QRVQIRLVVI QVLVFSLLLT LGGRLWYLQI RNGDEYTAEA AGNGVQQVVQ
PAVRGSILDA RGVPLADNET RLVVSASRTE LLKMKDDGVG VLARLADVLD MKAQDVRDKV
RLCDAKTPQP CWNGSPYQPI PVTDEATTQQ ALTIRERAED FPGITAEPTA VRRYAAPGKA
KTAQVLGYLS PVTDDEIQKA QDGPSPYLRS DQVGRSGLER TYDKELRGKA GVTRYEVDNL
GRVMGEAEND PAVPGSNLVT SLDARIQAVA EYELAQAMKT VRQETDKITG RKYEADSGAV
VVMESKTGRV VSMASQPDYD PNDWVGGISG KQYAKLTSKK SNYPLLNRGI QGQAPAGSIF
KVVSASAAVR AGHDFDDLYD CSSSYSLGSQ TFANFESQGH GPITLGDALK YSCNTVFYRL
GHEQWARDGG MKPKKDAKDW FYRTARDFGL GAETGIDLPN EVKGRIPDRN WKQDFWKANK
DAWCKEGKKG GTYVQQIAYE SCLEGNQLKA YDSINYAIGQ GDVLVTPIQM ATAYAAISNG
GTLYEPTVGK AVISPDGKTV QEIKPKARGK LPVDAQTVKD LDKGLRSVVE PGGTAAWRFG
GWPQDKIPMH AKTGTAQVYG KQTTSWFATY TDDYTIVMTI SQGGTGSGAS GPAVRKIYDA
IYGLDAEGNQ DVKKALLPKP QKALPTIQPD GSIHAPKVRP YDPRPAQPEG QEAGPEFVLP
QPSGQPGLTG SPATTGRRP
//
