ID A0A0G3GYI9_9CORY Unreviewed; 611 AA.
AC A0A0G3GYI9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:AKK06206.1};
GN ORFNames=CMUST_09450 {ECO:0000313|EMBL:AKK06206.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06206.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK06206.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06206.1,
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; AKK06206.1; -; Genomic_DNA.
DR RefSeq; WP_047262277.1; NZ_CP011542.1.
DR AlphaFoldDB; A0A0G3GYI9; -.
DR STRING; 571915.CMUST_09450; -.
DR KEGG; cmv:CMUST_09450; -.
DR PATRIC; fig|571915.4.peg.2000; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000035199; Chromosome.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR007887; MecA_N.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR Pfam; PF05223; MecA_N; 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:AKK06206.1};
KW Cell division {ECO:0000313|EMBL:AKK06206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199}.
FT DOMAIN 31..139
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 331..593
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 611 AA; 64418 MW; 4F4B689D0CDC4FE3 CRC64;
MNHSAVPALR FAVAACVAAG ILSGCTPKPL SAEPIVEDFL SQMAARHIQA AAGLTDKEEN
VAEVWEATWA GLQAEGLETE ITDVDIRDSL ATATYTLRWD LPKDRELVYD ASMTLNRINN
QWKIRWQPTA LHPKLGANQH LELRAINAQR ASIVSSDGIE ILAPGTVDRI LVDTGKTSDR
KATANAIAHA LDVAHAEDES VPQIDATELA KSLQSASGTY SVTTVNQQAG ARLRELLAEK
PGIIFNDEAA MVSKTPGFAP DIVSRVTKLV NEELEGANGW RVAVVTHDGA LIDDILYQAP
KLAPAVRVSL NHKVQLAAED AVNLRSEMKA MIVAIRPSNG EILAVAQTDK ADEEGDLALT
GQFPPGSTFK IITASAGIGQ SGLRSDSIVA CPGTMNIYGR TVTNYNGFSL GNVPLQTAFA
RSCNTTFADI STRLEAGELK RIGKEFGIGI DYDIPGLSTI TGSIPNGDTP LDKTEAGYGQ
GLTLVSPFGM ALVSATAAHG STPTPQLVSG FSTTQKETVP PPSPETIEEL RHLMGAVTEP
GGTAAGINAG GKIYGKTGEA EINGGSHAWF TGYRDDIAFA TLIVLGGGSE SAVAITDKFF
QRLDELSAPA G
//
