ID F7QYM8_9LACO Unreviewed; 688 AA.
AC F7QYM8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Penicillin binding protein {ECO:0000313|EMBL:EGM53382.1};
GN ORFNames=LRU_00518 {ECO:0000313|EMBL:EGM53382.1};
OS Ligilactobacillus ruminis SPM0211.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1040964 {ECO:0000313|EMBL:EGM53382.1, ECO:0000313|Proteomes:UP000002971};
RN [1] {ECO:0000313|EMBL:EGM53382.1, ECO:0000313|Proteomes:UP000002971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPM0211 {ECO:0000313|EMBL:EGM53382.1,
RC ECO:0000313|Proteomes:UP000002971};
RX PubMed=21742873; DOI=10.1128/JB.05601-11;
RA Lee S., Cho Y.J., Lee A.H., Chun J., Ha N.J., Ko G.;
RT "Genome Sequence of Lactobacillus ruminis SPM0211, Isolated from a Fecal
RT Sample from a Healthy Korean.";
RL J. Bacteriol. 193:5034-5034(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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:EGM53382.1}.
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DR EMBL; AFOJ01000002; EGM53382.1; -; Genomic_DNA.
DR RefSeq; WP_003694273.1; NZ_AFOJ01000002.1.
DR AlphaFoldDB; F7QYM8; -.
DR Proteomes; UP000002971; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; 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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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: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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..303
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 347..674
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 688 AA; 75158 MW; A8C8711880789205 CRC64;
MNFLKKANIN HDKKNKSHIP FRLNFLFFVV FILFAALIVQ LAYLQIVFGP RFESEAQSGD
TRTETKNVQR GMIYDSTGKI LVANNTSRAI TYTKPLMISS SDMFKIANNL IKYVEIEPSE
LSDSNKEDYY LANPKHEKFV KSQIKDAKKI TDSSKLYHME QDYVKKHKLG TKLTDSQKRA
ATVYAKMNGA YSLSTVYIKT KDVTDNEMAV VGENLSELPG IKIGTSWTRS YPNGDSVKSV
IGTVTTEKQG LPSDMINTLL AEGYSRNDSV GSSYVESQYE NVLKGTKEVI NVETRNNKIV
KEIKQYGGKA GDNVELTINS DFQNKVQKIM NDCVKSIVGG NPYSPGGYAV VMNPNTGGIY
ALAGVNRNVK TGKITDNALG AINQTYVMGS VVKGAMVLGA LKSGVITPSN NTLTDEPIKL
KGTATKSSWF NKTGGANLSL TASDALEVSS NSYMMKLAMM EGGFNYVPGS ALSLSNSIFD
KLRSNFKQFG LGVKTGIDIP GEAKGFEGPA NQAHIGNALD LSFGNYDSYT TLQLAQYIST
IANGGYRLQP HLLKSIRSTK RDGSLGEVRY EFEPNVLNVV GATDSQWNIV KEGLWKVVHG
TSSYRTGTRL ADIKPAVCAK SGTAQTFYNT AETETLSLVT YAPQKNPQVA IAVAFPDISD
SSSSINATAV KEIYDAYWKT VQTSDGLK
//
