ID C7M684_CAPOD Unreviewed; 619 AA.
AC C7M684;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:ACU92950.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ACU92950.1};
GN OrderedLocusNames=Coch_1404 {ECO:0000313|EMBL:ACU92950.1};
OS Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / NCTC
OS 12371 / VPI 2845) (Bacteroides ochraceus).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU92950.1, ECO:0000313|Proteomes:UP000006650};
RN [1] {ECO:0000313|EMBL:ACU92950.1, ECO:0000313|Proteomes:UP000006650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC {ECO:0000313|Proteomes:UP000006650};
RX PubMed=21304645; DOI=10.4056/sigs.15195;
RA Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT 2845).";
RL Stand. Genomic Sci. 1:101-109(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP001632; ACU92950.1; -; Genomic_DNA.
DR RefSeq; WP_015782537.1; NC_013162.1.
DR AlphaFoldDB; C7M684; -.
DR STRING; 521097.Coch_1404; -.
DR GeneID; 29675011; -.
DR KEGG; coc:Coch_1404; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_10; -.
DR Proteomes; UP000006650; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:ACU92950.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006650};
KW Transferase {ECO:0000313|EMBL:ACU92950.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..210
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 247..577
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 619 AA; 69668 MW; FD4C764D445CF878 CRC64;
MRKYLLPIII LFVAVVFLVR LFFLQVIFHE ENTGIDNIAI ETVYDYPERG YIYDRNGELL
VSNQPAYDVM VVPSEVKTLD TLELCGLLEI SKEEFRERLI KARDYSRKKP SVIVHQLSKD
DYAVLQEKLR KFQGFYIQKR MLRSYLTHNA GNVLGYISEV NEWELKKNPY YLAGELIGRS
GVEKQYEEFL RGKKGVQFFQ KDKHNAAIER YKNGAMDTLP ITGQPLQLTI DINLQAYGEM
LMQHKHGGIV AIEPKTGEIL ALISAPTFDP ALLVGRERSK NYTALYNDSI AKPLYDRTLL
AEYPPGSPFK VINALIGLQE GVITPGSVFS CGGGYRFGGR IMRCHCGRSS NDLLHGIAFS
CNSYFANTYK RAIDMKTTSA VGMDKWNAHV RSFGLGGFLG ADLPTGRAGK VPNTALYDKQ
YGKGRWNGTT NISNAIGQGE LLTTPIQLAN VMAAIANRGY YYTPHIVKKI DNKITPFQEY
TVAKHTTIAP KNFEPVIRGM NMAYEQGTAR RTQIEGINIA AKTGTAENFI KVNGKRMQLT
DHSIFVAFAP IEDPKIAIAV FVENGYYGAR VAAPIASLMI EKYLKGEVYR CDLEKQMLEK
SLEDEYMKPY SGLPFTINR
//