ID A0A1V9K9P2_9ACTN Unreviewed; 754 AA.
AC A0A1V9K9P2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:OQQ16334.1};
GN ORFNames=B0675_03480 {ECO:0000313|EMBL:OQQ16334.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ16334.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ16334.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ16334.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ16334.1}.
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DR EMBL; MWFK01000001; OQQ16334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9K9P2; -.
DR STRING; 1955065.B0675_03480; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000192467; 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 Reference proteome {ECO:0000313|Proteomes:UP000192467};
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..657
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 684..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 81499 MW; 8227D2A57C4339C8 CRC64;
MTNIPETGRT PRVQIRLVVI QILVLSLLGT LGGRLWYLQI RNGDEYAKEA SGNHVQQVVQ
PAVRGSILDA RGVPIADNET RLVVSASRTD LLKMRDDGRA VLTKLAGVLG LKPKDVIEKV
RLCDAKTPQP CWNGSPYQPI PITDEATAKQ ALQIRERSED FPGISAEPEA VRRYAAPGQA
NTAQVLGYLS PVTDDEITKA KDTDSPYLRS DQVGRSGLER EYDKELRGKA GVTRYEVDNL
GRVIGQAKSD KAEPGENLVT SIDSRVQRVA EYELNDAMKV ARTQFDKITG ENYKADSGAV
VVMEAKTGRV VAMASNPSYD PNAWVGGISG KDYTALTGKK SNYPLLNRAI QGQSAPGSTF
KVISTAAAVE AGYAFDGHYP CTSSYSVGNQ VFKNFEGESF GPISLGRALE VSCDTVFYGL
SDNEWKRDGG INPKKTPKDY FYKAAHQFGL GKETGIDLPN EVTGRVPDRK WKADYWKANK
AVWCKTGKKG GTYVQQIAYE NCLEGNRMRE GDSINYSIGQ GDTLVTPIQE AAIYSAVSNG
GTLYAPTIGK ALVSPDGKTV REIKPKKNGK LPVDQATLRG INDAFAGVVT RGTAAWKFGG
WPQDKIPLHA KTGTAEVYGK QTTSWLATYS KDYTIIMTIS QAGTGSGASG EAVRKIYNAL
YGVSADGAID KKKALLATPQ KSLPKIESDG SIDSPEVSKD PVKDLKANDA LRDGTTDPGQ
DLPAGTTPSP TAANRDTRRR SARRGKPRGK QVLT
//
