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Database: UniProt
Entry: Q68WH1_RICTY
LinkDB: Q68WH1_RICTY
Original site: Q68WH1_RICTY 
ID   Q68WH1_RICTY            Unreviewed;       594 AA.
AC   Q68WH1;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Cell division protein FtsI/ penicillin-binding protein {ECO:0000313|EMBL:AAU04021.1};
GN   Name=ftsI1 {ECO:0000313|EMBL:AAU04021.1};
GN   OrderedLocusNames=RT0553 {ECO:0000313|EMBL:AAU04021.1};
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363 {ECO:0000313|EMBL:AAU04021.1, ECO:0000313|Proteomes:UP000000604};
RN   [1] {ECO:0000313|EMBL:AAU04021.1, ECO:0000313|Proteomes:UP000000604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington {ECO:0000313|Proteomes:UP000000604};
RX   PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; AE017197; AAU04021.1; -; Genomic_DNA.
DR   RefSeq; WP_011191002.1; NC_006142.1.
DR   AlphaFoldDB; Q68WH1; -.
DR   KEGG; rty:RT0553; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_5; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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   Cell cycle {ECO:0000313|EMBL:AAU04021.1};
KW   Cell division {ECO:0000313|EMBL:AAU04021.1};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..229
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          262..585
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   594 AA;  66962 MW;  8647EBDAB3856C95 CRC64;
     MLNKKILHGE LISRRAFIIG LGKLWFLSLL GIRMFYLQLI KSEEYRTLSD KNRINFVVLP
     PIRGKIYDLD GNILATNKPC YQLVIDKSIN NNYRDELEII SNILNFSPDK YNYIKQKIKK
     SSRHTILTIL DHLDWEQVSM IEEQKHKLAA IFIDVGYLRF YPFSSTTSHL IGYLGQINEQ
     EKQELNIRSL SDFNIGKSGI EKYYDNKLRG EFGYKKVEVN AYGKQVRTIS ETPTQSGADM
     HLNIDASLQK KIQQYLNPKG SSAIVMDIRT GNVLICVSTP GFESNNFSKL SENYWQSLIS
     DPHKPLINKV IQNSYPPGSV FKIITVLAAL EVGINPNKTV FCDGSSILGT NSFRCWNHRG
     HGTLDMMSAL KYSCNIYMYE LARIVGPDKI LAVAREFGFG SKTGIDISPE SSGFVPSKEW
     KKKKLKLPWS IGDSFNLAIG QGFLGVTPIQ LARFITAIAS NGKLYTPRIL KNASEFYNVN
     IKTENIKIIQ ESLYNTVNVA GGTAYYNRIF AENRKLAGKT GTAQVQSKLN AKDDLNRDSI
     AWARRNHALF LGFAPYSDPR YSVTVFVDHG GGGSIAAAPV ARKIMSDVLD KYMR
//
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