ID C9R8K3_AMMDK Unreviewed; 646 AA.
AC C9R8K3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:ACX52632.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ACX52632.1};
GN OrderedLocusNames=Adeg_1537 {ECO:0000313|EMBL:ACX52632.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52632.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX52632.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP001785; ACX52632.1; -; Genomic_DNA.
DR RefSeq; WP_015739509.1; NC_013385.1.
DR AlphaFoldDB; C9R8K3; -.
DR STRING; 429009.Adeg_1537; -.
DR KEGG; adg:Adeg_1537; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_1_9; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000002620; 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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:ACX52632.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002620};
KW Transferase {ECO:0000313|EMBL:ACX52632.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 265..640
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 646 AA; 70729 MW; 06BBAC709B70FE60 CRC64;
MASPVEHKGK VFLLVCALLF TILFLRLGYL QIWRGEHYAV LAKENCLRLV LIRAPRGEVF
DRNGQKIVGN RPVYALSYVN LGKPVAPDLV KRLAGLLNMD PAEIEKKIKE GENSGQPVRL
ATNVPLQAVT YLEEHHDEFP GIMVEIVPVR YYPYGSVLAQ VLGYVHEISA EQLKKHKDEG
YAPGDFFGQD GLEYAFERYL RGKDGARYIE VDAVGRPVRD LGVKPPTPGD NLELTIDLKV
QQAAEAALEK AVKEARKKGF PAPGGAAVVE DVHTGEILAM ASYPSYDPSV FTRGLTPVEA
KALFQNPDSP LLNRALSAYP PGSTFKMVTA LAALEAGIIN PDFTVFCSGY YRLGSHIFRD
WLSSGHGTVN LKRALQVSCN VYFWTVGQMT GIDRLARMAR ELGLGEKTGI TLPGEMAGVV
PTPEYKYKRM KAYLDSIFEP KFKAVEEEYA RKLKATQDPK EREKLEKEKD RRLQALRAEY
QRYAWDLDWH TYDTLNTAIG QGYVSCTPLQ LVNYTATLAN GGTRYRPFLV KKIVAPDGRT
VASFGPEVLG RLKVKPEYLK AVQEGMSLVT QGDGTAAGVF NGLPVKVAGK TGSAEVPGKG
TCALFVGYAP ADNPRVAVAV VVENAGHGGA VAAPVAKEIL SAYFGG
//
