ID A0A147K9S4_9BACI Unreviewed; 635 AA.
AC A0A147K9S4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=Q75_05645 {ECO:0000313|EMBL:KUP07198.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP07198.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP07198.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
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:KUP07198.1}.
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DR EMBL; LDYG01000024; KUP07198.1; -; Genomic_DNA.
DR RefSeq; WP_059350814.1; NZ_LDYG01000024.1.
DR AlphaFoldDB; A0A147K9S4; -.
DR STRING; 1150625.Q75_05645; -.
DR PATRIC; fig|1150625.3.peg.1184; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000074108; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06573; PASTA; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF19; STAGE V SPORULATION PROTEIN D; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
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; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT DOMAIN 578..635
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 635 AA; 69436 MW; E66259F59B8D61D5 CRC64;
MSSVTVRKRL ALILVGGLMI FGIIDFRLAY VQFIMGNGLT SEAKELWSRN IPFEPERGKI
LDRNGVELAT NQSSPTVFVV PRQVKDPTAT AERLAASLNM NVEKAYEYIT KVASIVRIPE
GRKISYEKAQ EIEGLKLNGV YIGEDSTRYY PYGSYLSHVL GFAGIDNQGL MGLELSYDKA
LSGDKGYVQY YSDAKGQKMP DMADDYAEPV DGLDLYLTID TQIQTIMERE LDNAEALYNP
DGIVAIAMDP NTGQILGMSS RPNFDPGSFQ DVSPEIYNRN LPIWSTYEPG STFKIITLAA
ALEEEVVDLH NENFYDSGHV EVGGSTLHCW TRGGHGDQTF LEVVQNSCNP GFVELGQRLG
TETLFSYIDA FGFGKKTGID LQGEGAGILF DIDRVGPVEL ATTAFGQGVA VTPIQQVVAV
AAAVNGGTLY QPYVAKELVD PKTGEVVMRN SPVAKGQVIS QETSKQVREA LESVVALGTG
GGAYVDGYRV GGKTGTAQKA ENGRYLENNH IVSFMGVAPM DDPKVVLYLA VDNPKGTVQF
GGVVAAPIVG NMMEDIMHAL EVEPRKEQIE KEKRTWQDIP YIEVPNLIGL TKKELSQQLL
NFQLEAEGEG NQVVQQSPDP GTRVQEGSKI RVYFE
//
