ID   M1NZ50_BARAA            Unreviewed;       583 AA.
AC   M1NZ50;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AGF74722.1};
GN   Name=ftsI {ECO:0000313|EMBL:AGF74722.1};
GN   OrderedLocusNames=BAnh1_08460 {ECO:0000313|EMBL:AGF74722.1};
OS   Bartonella australis (strain Aust/NH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74722.1, ECO:0000313|Proteomes:UP000011729};
RN   [1] {ECO:0000313|EMBL:AGF74722.1, ECO:0000313|Proteomes:UP000011729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74722.1,
RC   ECO:0000313|Proteomes:UP000011729};
RX   PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA   Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA   Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT   "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT   the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL   PLoS Genet. 9:E1003393-E1003393(2013).
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DR   EMBL; CP003123; AGF74722.1; -; Genomic_DNA.
DR   RefSeq; WP_015398229.1; NC_020300.1.
DR   AlphaFoldDB; M1NZ50; -.
DR   STRING; 1094489.BAnh1_08460; -.
DR   KEGG; baus:BAnh1_08460; -.
DR   PATRIC; fig|1094489.3.peg.1022; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_2_5; -.
DR   OrthoDB; 9789078at2; -.
DR   Proteomes; UP000011729; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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   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        35..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..186
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          247..536
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   583 AA;  64590 MW;  3580707AFDE9735D CRC64;
     MKLSFPFPRK KTRLNSQSNF KNFPIHRSYS DRPRLIFSLL CFLVLYGIMG WCLISYGLED
     GQIEETKGPV VPQLATRPDI VDRNGRLLAT DIKTYSLFAE PRRIVDVDET IELISTVLPK
     LNWQETYRRL KRKSGFSWIQ RGLSPTQKTK IMALGIPGVG FRTEIRRFYP DGPVASHILG
     MVNVDNQGIA GIEKYIDDTG LSVLRETGLV SETSLKPVQL SIDVRIQAIV RSELMKAMER
     YKAIAAGAVI LNIRTGEVLA MASVPDFNPG NPVDALKSNR LNRMTAGTFE MGSIIKSFTT
     AMALNSGIFH LNSVIDASKP IQAGRGYFIH DFHGKNRPLT LKEVFIYSSN IGSAQEALAV
     GVDRHRDFLK RLGLLDRMTI ELPEVARPIE PRHWRDINSM TISFGHGMAT TPLQTAAAAA
     ALMNGGWLIG PTFLMRTEEQ ALKHAKQVVK SQTSRDMRYL YKLNSSIGSG RNARVEGYRV
     GGKTGTAEKV ENGKYSTTKN FNSFLAAFPI DDPSYVVLTI IDEPQPEVGK HSATAAMNAG
     PTLANIIRRS ASFLGIKSDF KKEYEAISGT GGDLRLAKTT VKN
//