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Database: UniProt
Entry: Q1ZAP6_9GAMM
LinkDB: Q1ZAP6_9GAMM
Original site: Q1ZAP6_9GAMM 
ID   Q1ZAP6_9GAMM            Unreviewed;       684 AA.
AC   Q1ZAP6;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000256|HAMAP-Rule:MF_02081};
DE            EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02081};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_02081};
DE            Short=PBP-2 {ECO:0000256|HAMAP-Rule:MF_02081};
GN   Name=mrdA {ECO:0000256|HAMAP-Rule:MF_02081};
GN   ORFNames=P3TCK_03696 {ECO:0000313|EMBL:EAS45446.1};
OS   Photobacterium profundum 3TCK.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS45446.1, ECO:0000313|Proteomes:UP000003789};
RN   [1] {ECO:0000313|EMBL:EAS45446.1, ECO:0000313|Proteomes:UP000003789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3TCK {ECO:0000313|EMBL:EAS45446.1,
RC   ECO:0000313|Proteomes:UP000003789};
RA   Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA   Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02081};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02081}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02081}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
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:EAS45446.1}.
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DR   EMBL; AAPH01000001; EAS45446.1; -; Genomic_DNA.
DR   RefSeq; WP_006228749.1; NZ_CH724134.1.
DR   AlphaFoldDB; Q1ZAP6; -.
DR   HOGENOM; CLU_009289_1_1_6; -.
DR   OrthoDB; 9766847at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000003789; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   HAMAP; MF_02081; MrdA_transpept; 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   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW   Rule:MF_02081}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02081};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT   DOMAIN          65..240
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          286..623
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        345
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ   SEQUENCE   684 AA;  77551 MW;  670D2594587E5030 CRC64;
     MHKEKVKIRD HQSEMSLFTR RAITAFLFML VGVGVLLTNL YHLQIENHSQ YQARSNNNRI
     KVIPVEPNRG RIYDRNGVLL AQNTPVYSLE LIPEKVHDMD ATLASLKSLL GLNEHDIAQF
     KKATHRTLRT RPVTLIEQMN EVQVAKFSVN QFQYDGVDID AYLERYYPYS ANLTHVLGYV
     GKINDRDIRR LKEEEKYTNY KATRTIGKLG IERYYEDTLH GESGYEKVEI DSRGRVVRTL
     DYVAPISGQD IKLNIDVGLQ LYANKLLTIK KENPITHKME DYHRRGSIVV LDPRDNSVLA
     MVSSPSYDPN LFVHGISSKR YNALLNDPDH PLLNRSTLGV YPPGSTVKPQ IAVAALSEGV
     ISPNTTRNFP GWWRIPHSKS RKFRDDVRWG HGEVNVVQAI EQSVDTFFYQ VAYDMGIDRL
     SVWMNKFGYG KPSGIDINEE STANMPTREW KHAHYHQAWY QGDTIPVGIG QGYWTASPMQ
     IAKATAVLAD EGVVHRPHLL KAVMENGQFE PVLFKDFPRI SEAKKQNWDL AIDGMHRVLV
     SGTARKLFKN LAYEAGGKTG TSQVFGLAKG QKYNSKEVAE HLRDHALFTG FAPLNHPKVL
     VAIVLENAGW GKYAAPLARN IMDYVLVKPT INLDTDPSNL PPDQLITHDG IHVNVQKNTQ
     TTLPKKELAH HKVKTLDSEQ VKHS
//
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