ID A0A0F0H3Z6_9ACTN Unreviewed; 723 AA.
AC A0A0F0H3Z6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KJK50235.1};
GN ORFNames=UK14_13790 {ECO:0000313|EMBL:KJK50235.1};
OS Streptomyces sp. NRRL F-4428.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK50235.1, ECO:0000313|Proteomes:UP000033569};
RN [1] {ECO:0000313|EMBL:KJK50235.1, ECO:0000313|Proteomes:UP000033569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK50235.1,
RC ECO:0000313|Proteomes:UP000033569};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK50235.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYJI01000101; KJK50235.1; -; Genomic_DNA.
DR RefSeq; WP_030027167.1; NZ_JYJI01000101.1.
DR AlphaFoldDB; A0A0F0H3Z6; -.
DR PATRIC; fig|1609137.3.peg.2929; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000033569; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000033569};
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 672..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 78722 MW; 904437E8BC3491E9 CRC64;
MTNVPETGRT SRVQIRLVIM QVLVFSMLIT LGGRLWFLQI RNGAEYYHEA KSNHVQRVVQ
PAVRGSILDA RGVPLADNET RLVVSASRTA LMKMKDKGRG VLTRLADVLD MTPKQVMDKV
RLCDSQTPKP CWNGSPYQPI PVTLEATTQQ ALQLRERPEE FPGITAEPTA VRRYPAPGGA
RTAQVLGYLS PVTDDEIQKA KDTDSPHLRS DQVGRSGLER TYDRQLRGKA QVTSYEVDNL
GRVMGQTRSD PGIAGSTLVT SIDARVQAVA EYELQQAMKV VRNETDNITG RKYEADSGAV
VVMEAKTGRI VAMASQPDYD PNAWVGGISG ADYAKLTSKN SNYPLLNRAI QGMAPAGSIF
KVVSASAAVR AGYKFNDRYN CSSSYSLGGR SFANFESKGH GPITLGEALK FSCNTVFYAL
GHKEWQRDGG LSPKKDAHDW FYRTAREFGL GSETGIDLPN EVKGRIPDRQ WKQSFWAANK
NSWCKQGKRG GTYVEQIAYE SCLEGNQLKA YDSINFAIGQ GDVLVTPIQM ATAYSAISNG
GTLYNPTVGK AVISPDGKHV EILKPQSHGR LPVNAQTVAD LDRGLRMVVE PGGTAAWRFG
GWPQDKIPMH AKTGTAQVYG KQTTSWLATY TKDFTIVMTI SQGGTGSGAS GPAVRNLYNA
LYGLTMDGKP NQKGALLPAP ETKLPKINPD GSIESPEIRP YVPPSPEDLQ APALAGPPPT
RHD
//