ID C4LKM4_CORK4 Unreviewed; 557 AA.
AC C4LKM4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative penicillin-binding protein 4 {ECO:0000313|EMBL:ACR18379.1};
GN OrderedLocusNames=ckrop_1654 {ECO:0000313|EMBL:ACR18379.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18379.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR18379.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP001620; ACR18379.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LKM4; -.
DR STRING; 645127.ckrop_1654; -.
DR MEROPS; S13.004; -.
DR KEGG; ckp:ckrop_1654; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_017692_0_1_11; -.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 243..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 56768 MW; 6A98363A7E40F494 CRC64;
MPRWRTGAIS AFLSTFPSPR IGPEGEVFRV VSGVSAKLTT VKKGKKNSGG STAVRTGSFR
RSAVSSVLTV LTIIVVAAVI VGAVVMYQQR NAYTSAKPAG PVDSGVSVSG PNADAPIPDI
TKALQGPASN GALGQLAGQV TDASTGKTLW EKNSSTAMVP ASSTKMMTTA AALLTLGPKD
RVRTVVKRGT KPGQIVLVGG GDVTLAASKD NAFYTNAPTI QDLASQVKKN MGGQPVTSVV
VDNSRAGQGD TFNSTWSRGD ISGGNVTSVD SVMLNGGRQD PSDADSPRTD NPALVAGQAL
ANALGLSSSS SDDGNGADNA GDSGDFGESN DESGNSGGGD DNSQGVSVSK KSVDTEDGEL
GAVESAPLDI RIHDMLVNSD NMEAEAIGRE IAKKEGKPLT FEGATSATKE VLSQHGFPLE
SVVLKDNSGM SPDNRITPRL LDRIMVKASS PVTNEGNSDS SSADSQSHDL RPILDGLPVA
GGNGTLAGRF TPGSSSGPGA GWVRAKTGTL DGVSALVGTV MNQQGRVLTF AFMSNGSDIE
PARSALDDLA SALRTSS
//
