ID K5BFR9_MYCHD Unreviewed; 582 AA.
AC K5BFR9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Penicillin binding transpeptidase domain protein {ECO:0000313|EMBL:EKF23381.1};
GN ORFNames=C731_2632 {ECO:0000313|EMBL:EKF23381.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF23381.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF23381.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF23381.1}.
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DR EMBL; AMRA01000071; EKF23381.1; -; Genomic_DNA.
DR AlphaFoldDB; K5BFR9; -.
DR STRING; 1122247.GCA_000379865_02095; -.
DR PATRIC; fig|1122247.3.peg.2528; -.
DR eggNOG; COG0768; Bacteria.
DR Proteomes; UP000006265; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 35..198
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 242..554
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 260..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 62277 MW; FE22A970C35A1FDD CRC64;
MLVLAAAQLF NLQVPRAEGL RKEAASQLKV TDVDKAVRGA IIDRDNDKLA FTIEARALTF
QPKKVRQQLT EAKAKSPDAP DPDQRLREIA DEVAARLNNK PNAATVLKKL RSDETFVYLA
RAVDPAIAEA ITDKFPEVGA ERQDLRQYPG GSLAANIIGG VGWDGHGLLG LEDALDAVLA
GTDGSITYDR GSDGVVIPGS YRNRHEAVDG STVQLTLDSD IQFFVQQQVQ LAKEVSGAKR
VLAVVLDAKT AEVLAMANDN TFDPSQDIGR QDDRELGNPS VSAPYEPGSV NKIVTAASVI
EFGLSHPDEV LQVPGSIAMG GVTVRDAWAH GTVPFTTTGV FGKSSNVGTL MLAQRVGPER
FVEMMRKFGL GQRTGVGLPG ESAGLVPPIA QWSGSTFANL PIGQGLSMTL LQLAGMYQAI
ANDGLRIPPR IVKATIAPDG TRTEEPRPEG IRVVSPETAR TVRHMFRSTV QRDPRGVQQG
TAPQAAIEGY QVSGKTGTAQ QINPACGCYY DNVYWISFAG MVPADNPRYV IAVMADNPQR
TSDGQPGSTF APLFQTIASW LLQRENVPLS PDPGPPLTLQ AT
//
