ID M8D811_9BACI Unreviewed; 726 AA.
AC M8D811;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=H919_02817 {ECO:0000313|EMBL:EMT46997.1};
OS Anoxybacillus flavithermus AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1297581 {ECO:0000313|EMBL:EMT46997.1, ECO:0000313|Proteomes:UP000012085};
RN [1] {ECO:0000313|EMBL:EMT46997.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT46997.1,
RC ECO:0000313|Proteomes:UP000012085};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Anoxybacillus flavithermus AK1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMT46997.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT46997.1,
RC ECO:0000313|Proteomes:UP000012085};
RX PubMed=26044438;
RA Khalil A., Sivakumar N., Qarawi S.;
RT "Genome Sequence of Anoxybacillus flavithermus Strain AK1, a Thermophile
RT Isolated from a Hot Spring in Saudi Arabia.";
RL Genome Announc. 3:e00604-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:EMT46997.1}.
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DR EMBL; APCD01000002; EMT46997.1; -; Genomic_DNA.
DR RefSeq; WP_003395096.1; NZ_APCD01000002.1.
DR AlphaFoldDB; M8D811; -.
DR PATRIC; fig|1297581.3.peg.576; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000012085; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR Gene3D; 2.20.70.70; -; 1.
DR Gene3D; 3.30.70.2110; -; 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; IPR005543; PASTA_dom.
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; PF03793; PASTA; 2.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR PROSITE; PS51178; PASTA; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:EMT46997.1};
KW Cell division {ECO:0000313|EMBL:EMT46997.1};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 586..646
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 647..703
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 707..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 80793 MW; 9B1E9F3463C70A39 CRC64;
MRKHTHTHRG AAIYFGLFSL LFFILFGRFV YLQATGVADG QVLAVEAQKR YLKKQVLEAK
RGTIFDRRGE VIAEDIPSYT VAAILDPDMP QHVSDPETTA RKLAPLLNMD VADVERILKK
NAKQVEFGPN GRGVSQTVKK EIEALQLPGI IFLRDSKRFY PNGTFASYVV GYAQKNEETN
EVEGKMGIEK QFDEQLKEKD GYVVYEGDQQ GFKLPHADEK IVPPQNGKDI YLTIDKHIQT
FLEDAMNAVE KQYAPKKMIA IVADPKTGAI LAMSTRPSFN PNKRNIENYF NDAIAYPYEP
GSTMKIFTLA AAVNEGVFPA NETYLSGSYQ VGSHRIRDHN KVGWGKITFL EGVQRSSNVA
FAIIVREKLG EDRFLQYLHR FRFHEPTGID LPGEKVGNIL YRYPIEKVTT GFGQGTSVTP
IQQIQAATAI ANGGKMMKPY VVDRIVDSES GKTVVKHEPQ VVDTPISKET AEKVLDILET
VVTSEKGTGR PYQIEGYRVA GKTGTAQIPD PKGGYLTGHQ NYIFSFLGMA PRENPRLIMY
VAVQQPNISY TETGAAPVSM IFNSVMKSSL QYLNIQPTAE KKSEKKEKSV TLSSYVGQSV
EQAVQSLENE GLHVTVIGKG KRVHAQFPRA GERVVAPDRV LLQTDGNAIM PDLTGWSLRD
VMKLAELLQL KPSFIGSGYV FRQNISPGAV IKQNDYVIVE LAKPSELSEK KENKESEQQE
ADGPID
//
