ID A3PA91_PROM0 Unreviewed; 548 AA.
AC A3PA91;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Putative penicillin-binding protein {ECO:0000313|EMBL:ABO16666.1};
GN OrderedLocusNames=P9301_00431 {ECO:0000313|EMBL:ABO16666.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO16666.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO16666.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO16666.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP000576; ABO16666.1; -; Genomic_DNA.
DR AlphaFoldDB; A3PA91; -.
DR STRING; 167546.P9301_00431; -.
DR KEGG; pmg:P9301_00431; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_3; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0016020; C: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: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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430}.
FT DOMAIN 13..182
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 217..541
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 548 AA; 60867 MW; E01C1937810FB96A CRC64;
MSDENRIRLI ASQPIRGRIL DKNGYVLADS RVKYSLIIKP QSVIKSNWEK HKSSLSNLLN
IDSNEIQKIY SDGLKNQKLS ATILDDLNVD QLIKFKENQD NLISFEIASK LIRNYPYKSL
AAHVIGYTQP ITESEYKFLS KKGYKLNDLI GRTGIEYVYE DFIRGEWGGE MVEVNSLGKF
QRSLGIRPPV QGNDIQLTID LNLQLVAEEV LKDKKAGAVI VMDPRDGAIR AMTSKPTFDL
NFFSKDFKPE KEYNKLFNSP EKPLFNRALN AYDPGSVWKI VTALAGLESG KFPRETMLDT
KACITYGSQC FREHNDLGFG LIGYEDALRV SSNTFFYQVG YGVGVDEIHK IARKLGFNSL
SGIEISEQEN IGLVASSEWA KEGRGWGQPG RTPWVPEDIA SMSIGQFVVQ VTPIQIARAY
AAIANGGYLV TPYLVKKDDV NLSDKKLTKI DIDSNNIQLI KSGLRKVVES GTGVSINYGV
SNLPPVSGKT GTAEDGEGGL DHAWFVCFTP SEKSELLVVA FAQNTPGGGS VHALPMAREI
LKVWNEKE
//
