ID I0ES55_HELCM Unreviewed; 614 AA.
AC I0ES55;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:AFI05774.1};
GN OrderedLocusNames=HCD_03790 {ECO:0000313|EMBL:AFI05774.1};
OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI05774.1, ECO:0000313|Proteomes:UP000005013};
RN [1] {ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFI05774.1, ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RX PubMed=24358262;
RA Kersulyte D., Rossi M., Berg D.E.;
RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum
RT Strains from a Dolphin and a Whale.";
RL PLoS ONE 8:E83177-E83177(2013).
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DR EMBL; CP003481; AFI05774.1; -; Genomic_DNA.
DR RefSeq; WP_014659283.1; NC_017735.1.
DR AlphaFoldDB; I0ES55; -.
DR STRING; 1163745.HCD_03790; -.
DR KEGG; hcm:HCD_03790; -.
DR PATRIC; fig|1163745.3.peg.804; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_4_7; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000005013; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 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; 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 Cell cycle {ECO:0000313|EMBL:AFI05774.1};
KW Cell division {ECO:0000313|EMBL:AFI05774.1};
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 24..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 282..589
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 614 AA; 69276 MW; AEB606E8D7BDD993 CRC64;
MDTKNIETSF NSERFLQTQK YKSVLTTLVF LVLFLFFLVV AFIKAVFPRT NMPTLIISKQ
DVATRGTIYS QDNYSLASSQ KLFKLGFDTR FLNPDKKDFF IDFLSIYSNI SKKSLKNALN
TKGYTTLAYD LTPNTAANLK DLNKKFLAFG VFQNFKDKHN KVWQKQGLDI EVSGVSRHYP
YQSSLEPIVG YVQKQEEEKL TLTTGKKGVE KSQNHLLKAQ QNGIRTGKRD VSFNFIQNHS
YTEHERLDGY EVYLSIPLKL QKEIETLLDA AKDKLKAKEI LVGIINPKSG EILSLATSNR
FNPNTIKTSD YENLNLSIAE KVFEPGSTIK PIVYSLLLEK SLINPKERIN LNNGYYQLGK
YTIKDDFIPS KKATIEDILI KSSNVGMIKI TQNLSPKDFY NGLLGYGFAQ KTGIDLSLEA
TGKIPPLNAF KREVLKGSIS YGYGLNATFL QLLRAYAVFS NEGKLCTPYL VQRKTAPNGD
IYIPSQKPAF QAISQKSARK MRKTLLKVVR YGTGKNAQFE GLYVGGKTGT ARIAKNGSYS
EESYNSSFFG FVEDERQVFT IGVVILGSHG KEEYYASKIA APIFKEITEI LVRYHYLSPS
IAIQNALEKT KNTK
//
