ID C3PNZ7_RICAE Unreviewed; 560 AA.
AC C3PNZ7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:ACP53657.1};
GN Name=pbpA2 {ECO:0000313|EMBL:ACP53657.1};
GN OrderedLocusNames=RAF_ORF0778 {ECO:0000313|EMBL:ACP53657.1};
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255 {ECO:0000313|EMBL:ACP53657.1, ECO:0000313|Proteomes:UP000002305};
RN [1] {ECO:0000313|EMBL:ACP53657.1, ECO:0000313|Proteomes:UP000002305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5 {ECO:0000313|EMBL:ACP53657.1,
RC ECO:0000313|Proteomes:UP000002305};
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(2009).
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DR EMBL; CP001612; ACP53657.1; -; Genomic_DNA.
DR RefSeq; WP_012719850.1; NC_012633.1.
DR AlphaFoldDB; C3PNZ7; -.
DR KEGG; raf:RAF_ORF0778; -.
DR HOGENOM; CLU_009289_6_2_5; -.
DR Proteomes; UP000002305; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; 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 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..193
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 240..522
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 560 AA; 63027 MW; 5EB0101ADFCCEE23 CRC64;
MKQIWEKWKP TIKSLTIWNV CSKNTKIRLL MVICVFSFLF CTLSYRLIIV ATNVYDKNIN
SFKKNHQFRK EIVDRNGNLL AVNLPSASLF ANPQIVLDPE TSVKKLAEIL PDINKAKLLA
ELKSNKSFIW VKRDVLPSQQ EKITSLGLLG FEFEEEQKRI YTFSNLLSHV VGYVGRDSVG
LSGLELAYDK YLTNSDYELN EPKNRKEPLQ LSIDIRLQSI LSEEIDKTLK QFKAIGAVGI
IADPNNGEIL ALVNKPDFDP HYPSLAKPEE LFNIASLGIY EMGSVFKALT MAVGFDTGAI
NMNDAYDISY MKVGGFQLKD YTPRQGWHSV PEIFLYSSNI GTSQIMLEIG KSNFKKYLKK
LGLLDQLQIE LPERGTPLFP SEKRWNELTS VTMSYGYGIS ISPLHFVRAM LPVVNGGTLY
DLTLLKRKDE KVIGTKVFSE NTSTQMKKLF RAVVKEGNGK RAEVKGYLIG GKTGTAEKLS
QGAGKKKYLK NSRASSFLGM LPASNPQYVI FIRFDEPKPT KESFGFATAS WTAAPTAGRV
FERMISLYGL EPIEQSEEES
//
