ID A0A1Q7WWZ8_9CHLR Unreviewed; 594 AA.
AC A0A1Q7WWZ8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUG45_02255 {ECO:0000313|EMBL:OLE35262.1};
OS Ktedonobacter sp. 13_1_20CM_3_54_15.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805224 {ECO:0000313|EMBL:OLE35262.1, ECO:0000313|Proteomes:UP000186882};
RN [1] {ECO:0000313|EMBL:OLE35262.1, ECO:0000313|Proteomes:UP000186882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE35262.1}.
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DR EMBL; MNJJ01000040; OLE35262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7WWZ8; -.
DR Proteomes; UP000186882; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..222
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 266..579
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 594 AA; 64445 MW; F3F134CA74B072E9 CRC64;
MSIELRRARN RQMLIFLLVC VGMVALIGRL YFWQVVRGYG AADCTHGYGL AQCANLEHIQ
NQQLNAPRGL IYDAQGHILA TNVVRDDVYI EPYQFSADHS ADTFQSELAK LVDTLHRVLP
AVSQETLYKD FNLGYQTVRI ASRIDPTQSE KLRRLQLPYV FLEPRTWRIY PGGTLAAQVL
GYVQQDDQKS NGIYGIERQY NTLLTGKPGS FTAEFDLSGN PLVVGASSEQ PAVNGADLTL
TIDSSMQYMT QTALADTVKQ LGAESGTALV INIRTGAIVV MAGAPTFDPN QYGKSATLTG
CLGQESVFFN PVVYCAYEPG SIMKAVTMAA ALDQGLITPD TTFDDPGYRT FNDAPMVVNW
NGLAYGTESM TQVLEHSANV GAAYVAHDIL GANRYYPYLA KFGFGQATGI SPQEETGSYR
TPTNSPRLWS PSDLTRQAFG QSIFATPLQV AMAYATIANS GVMMHPYLVS AINNNGRIVT
TQPEALRRVI SAHAATLLTS MLMHSATNGL AQPAQVPGYT IAAKTGTATT QGLTSDKTEA
SVAGFIPATN PLFVILVKID RPQATIYGGT AAAPLWKAIG QQLMWYYHIP PDAP
//
