ID M7A8J1_9ACTN Unreviewed; 598 AA.
AC M7A8J1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:EMP12907.2};
GN ORFNames=ISGA_3793 {ECO:0000313|EMBL:EMP12907.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP12907.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP12907.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP12907.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP12907.2}.
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DR EMBL; APHK02000065; EMP12907.2; -; Genomic_DNA.
DR RefSeq; WP_053777367.1; NZ_CP132196.1.
DR AlphaFoldDB; M7A8J1; -.
DR STRING; 1241906.ISGA_3793; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:EMP12907.2};
KW Cell division {ECO:0000313|EMBL:EMP12907.2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 50..213
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 257..573
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 62826 MW; EF8879D506496E89 CRC64;
MFTLRSRIAW VVIVLAVLAV AVRMVIVHTI ESSSLSAQAA EQREYTQVLT AKRGSILDRN
GRPLAYTDEA RSLTFLPQVV RKTIGAAHHD NPELPDVDTR LKEISAGVSS ALGGSISADD
LLAKLKSDDT FVYLARSVSP DVAARITSEF PEVGADPQSI RLYPGGSLAA NVVGDVNYDG
NGLIGLEASL DSILAGTNGS RTYDRGSDGA VIPGSTRNVH PAINGATVRL TLDSDIQWFV
QAEVAKAKKA SGAKSASAVV LDSRTGEVLA MANDGTFNAS RPLDEQPDAQ LGNPSVTSPF
EPGSVNKIIT AAAAIEYGLT TPDQVHQVPG SIRMAGVTVN DAWTHGVEPY TTTGIFGKSS
NVGTLMLAQQ VGEERFADMV TRFGLGRSTG VGLPAESAGE VPALSQWSGG SFANLPIGQG
LSMSLLQMTG MYQAIANNGL RIPPRILMSE QRDGQGAEDE QRPDGVQVVS PQTAQTVRNM
FRAVLQDDPM GVQMGTGAKG AVAGYQLSGK TGTAQQVDPA CGCYSTSSYN ITFAGIAPAD
NPRFVVGIML DNPKRSSDGS GGQSAAPLFA TITSWILQHD RIPQSATQTP RLTLQASR
//
