ID A0A0G3GZ90_9CORY Unreviewed; 622 AA.
AC A0A0G3GZ90;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:AKK06486.1};
GN ORFNames=CMUST_10850 {ECO:0000313|EMBL:AKK06486.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06486.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK06486.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06486.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP011542; AKK06486.1; -; Genomic_DNA.
DR RefSeq; WP_047262506.1; NZ_CP011542.1.
DR AlphaFoldDB; A0A0G3GZ90; -.
DR STRING; 571915.CMUST_10850; -.
DR KEGG; cmv:CMUST_10850; -.
DR PATRIC; fig|571915.4.peg.2309; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000035199; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Cell cycle {ECO:0000313|EMBL:AKK06486.1};
KW Cell division {ECO:0000313|EMBL:AKK06486.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 48..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 280..598
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 622 AA; 66906 MW; 174D61BA8D0A5D86 CRC64;
MLSRLRWVQV IAIGVCVLLA GRMAWVQLVW GPELSQKAAD QRYRVYTDPA RRGEIQDRSG
QQLAYTMQAR SLTVSPKNLR KELRYVANND LAKSVDNYYG LSKEEREKRI DQKVLDYLDS
YSEEIPRIIA ETGASTSEIK SEEIRKKLDA DTTYEVLVRN VDPDVAVSIS EQHHGIAADI
QDIRQYPNGS VASNVIGKIS QDGQGQFGFE ASNDSLLSGI NGQTVVDVST DGQIIPGTTR
DQVAAMNGSD VTLTLDLDLQ TYVQQQLEQA KTNSGAKGAS AVVLDVETAE VLAMANTDAI
NPMGDIQKQL DRGKKFGNST VSEPFEPGSV AKIITAAGVI EDRLSTPDEV LTVPGSIDMA
GVNVKDAWDH GPTPYTTTGI FGKSSNVGTL MLAQRLGEQR FDSLLTGFGI GQTTGIELPS
ESAGLRPQLE QWSGGTFANL PIGQGMSLTL LQMAGVYQTL ANGGERIEPR IVAEIRDNTG
KVIEQPAPKK TRVVSESTAR TVVDMFRSVV QSDPAGIQQG TGAGAAVEGY QIAGKTGTAQ
QVDPNTGAYS NSKYWITFAG IAPADNPRFV VALMLDNPTR GVHGEGGQSA APLFHDIASW
LLDRDNVPLS PPAEGQLVLQ AQ
//
