ID I0H151_ACTM4 Unreviewed; 690 AA.
AC I0H151;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative penicillin-binding protein {ECO:0000313|EMBL:BAL86738.1};
GN OrderedLocusNames=AMIS_15180 {ECO:0000313|EMBL:BAL86738.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL86738.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL86738.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; AP012319; BAL86738.1; -; Genomic_DNA.
DR AlphaFoldDB; I0H151; -.
DR STRING; 512565.AMIS_15180; -.
DR KEGG; ams:AMIS_15180; -.
DR PATRIC; fig|512565.3.peg.1528; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_5_11; -.
DR Proteomes; UP000007882; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.30.450.330; -; 1.
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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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:UP000007882};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..309
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 362..667
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 74027 MW; 98D6EC468B0ED727 CRC64;
MAERGRLPRS GRTTDPFRPA LQVLDGGDTA PRARGRNQGA READEDGTDA RRSQREPAAP
RTKSAPRTKK EPEAAPRRRQ PTRPEKRPER KPEKARRPEK RVPAEPPKLA NSTRRLRLGT
VLALSLFVMI GVRLVVLQVA TSPDEAASLL ELRERRLSTV ELPAPRGSIL DRSGAVLAHS
VEARYVYVDP ENANLQKDVP GTAAKLAPLL RIQQSKLIEL MQRKQSLGRW LKFRYLARGV
DVAVADKIEA MRLPGIYTHT DERRDVPGKD LAANLIGFTG DDHHGLEGLE ARYDELLHGT
DGKRVFEVGK GSLGAPIPGG YERYTAAQPG NSLQLTIDRY VQYEVQRILD AQAEKNKATV
AGAVVLDART GEVLAQASYP AYNAAKPEAY DAQERIDVPT SVVTDPGSSH KAFIFGAALQ
EGLIKPDSTL TIGPALERGG EAFKDTHPQP KGTEMTMPGL LAYSSNVGTI LIGEKLGKEK
IYEYQQKFGL GQATGEGMPG EAEGMLLKPE DWSGSAPGSV PIGHSVSATL IQMAAAYGAI
ANDGTYIQPH LIKSTISGAD GKVTPAAEPK THKVLEPAVA SQLRTMMEAV VDAKGGTGGA
AAVTGYRVAG KTGTGKMLID GQYTSHNASS FIGMAPAEDP RYVIAVSMDV ATGGGGDVAA
PAFSEMMSYT LLHYFVPPSG TKPPTFKIHP
//
