ID   PODJ_CAUVC              Reviewed;         974 AA.
AC   Q9ZG88;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Localization factor PodJL;
DE   AltName: Full=Polar organelle development protein;
DE   Contains:
DE     RecName: Full=Localization factor PodJS;
GN   Name=podJ; OrderedLocusNames=CC_2045;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-585.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=10383964; DOI=10.1128/jb.181.13.3967-3973.1999;
RA   Crymes W.B. Jr., Zhang D., Ely B.;
RT   "Regulation of podJ expression during the Caulobacter crescentus cell
RT   cycle.";
RL   J. Bacteriol. 181:3967-3973(1999).
RN   [3]
RP   SEQUENCE REVISION, AND FUNCTION.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=12370432; DOI=10.1073/pnas.182411999;
RA   Viollier P.H., Sternheim N., Shapiro L.;
RT   "Identification of a localization factor for the polar positioning of
RT   bacterial structural and regulatory proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13831-13836(2002).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=15686556; DOI=10.1111/j.1365-2958.2004.04443.x;
RA   Chen J.C., Viollier P.H., Shapiro L.;
RT   "A membrane metalloprotease participates in the sequential degradation of a
RT   Caulobacter polarity determinant.";
RL   Mol. Microbiol. 55:1085-1103(2005).
CC   -!- FUNCTION: PodJL provides the positional information for the
CC       localization of several polar organelles (pili, adhesive holdfast and
CC       chemotactic apparatus) by recruiting structural (CpaE) and regulatory
CC       (PleC) proteins to a specific cell pole. {ECO:0000269|PubMed:12370432}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Note=Both
CC       PodJL and PodJS localize to the swarmer pole at different stages of the
CC       cell division.
CC   -!- DEVELOPMENTAL STAGE: PodJS, from the previous progeny, accumulates in
CC       the swarmer cell, and is partially degraded during the swarmer-to-
CC       stalked transition by sequential proteolytic cleavages (MmpA). PodJL,
CC       from the new progeny, is synthesized in the early predivisional cell,
CC       and then is likely to be converted to PodJS by proteolytic cleavage of
CC       periplasmic domain. After cell division, PodJL disappears, while the
CC       level of PodJS increases in the swarmer cell progeny.
CC   -!- PTM: Two isoforms exist, the full-length translation product PodJL and
CC       a C-terminal truncated form PodJS. Both appear during a specific time
CC       period of the cell cycle to control different aspects of polar
CC       organelle development.
CC   -!- MISCELLANEOUS: PodJS must be degraded to preserve the asymmetry of the
CC       next cell cycle.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72820.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE005673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF084609; AAC72820.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK000536; DAA00313.1; -; Genomic_DNA.
DR   RefSeq; WP_012640394.1; NC_002696.2.
DR   AlphaFoldDB; Q9ZG88; -.
DR   SMR; Q9ZG88; -.
DR   OMA; ITEAMPR; -.
DR   BioCyc; CAULO:CC2045-MON; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF08238; Sel1; 3.
DR   SMART; SM00671; SEL1; 3.
DR   SUPFAM; SSF47090; SSF47090; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Differentiation; Membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..974
FT                   /note="Localization factor PodJL"
FT                   /id="PRO_0000022081"
FT   CHAIN           1..?
FT                   /note="Localization factor PodJS"
FT                   /id="PRO_0000022082"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          757..793
FT                   /note="Sel1-like 1"
FT   REPEAT          794..829
FT                   /note="Sel1-like 2"
FT   REPEAT          830..865
FT                   /note="Sel1-like 3"
FT   REGION          460..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          81..163
FT                   /evidence="ECO:0000255"
FT   COILED          218..320
FT                   /evidence="ECO:0000255"
FT   COILED          375..469
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        468..488
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        291..292
FT                   /note="SA -> RP (in Ref. 2; AAC72820)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   974 AA;  103491 MW;  BB85D8DCEE9EE0B7 CRC64;
     MTAASPWSVK GIDPKAREVA KDLARRSGMT LGEWLNRMII EGDGQTADPR LAGDDVPNRA
     YLEIVKDDAP PRIEIAEHPA DEVGRVALAL DRLTQRIEAA EGRNAAAITG IDHSVRDALT
     RLGASEREQI AVAARFEGAV DELKTEQARA TERLRRIESE AAGPRSAEAL RALEGALGKV
     AGHLYEGEAR TREAIATLEA KLNQQSSGDP SALVEAVVAR LGERLEAAET RTSDALRELG
     ASFQALDQRL GAVETANPAT GVQEGLDSLA ATLTQKMEAA RLEMAAKLRE SADGRFDRME
     RKLGEMAAHV QAAEQRSAQA IERMGREIVG VADAFNRRVH AAESRNASAI EQVGGEVARI
     AASVEHKLNR ADSVQAQALE KLGGEIARIT EKLAERIGSA ERRNALAIDD VGEQVARVTE
     RLNQRHERSS QELVDRIRQS EERTLRMLEE AREKIDSRLS EAQRKLEAAP PSPPPAQAPA
     PVATAQRPVP PAASPFEDNY FSQAASFSTS EDEADAFDAP PAPARSFEVA EFPAAEPEEP
     AFAHDDYAIA DGFEPESPRY EVEPEVSDFA PAEPSRPMST RDIIEQARAA ARAAAASEGK
     GGKAKSAKKE KASKASGSLF SGFGGFSTKK SKARLGATVT TALVVFAAAG ALGAGVGGLL
     LLNTDDGNNS PSRVAQAIAG RKADVEVNGP EADTTPGAPR AAVALTTGKV VPAEVEAPAA
     PPTNEAKALF EDAVRKIESG DRSGVELLKR AANGGYPAAQ FYLSKMYEGG KNGVKVDMAE
     ARRWSERAAN GGDPRAMHNL ALYYFKGEGG PRNSTTAASW FRKAADMGLV DSQFNLAQLY
     ESGLGVSQNP AEAYKWYVIA GRAGDSTARG RATALRSQLT AEAQQTADRS ALAFRPQTQV
     QTASLSSAAP AAANANLGVA QRVLSQLGYY QGPRDGVSSP ALRMAIAAYQ RDQGLPPTGS
     VDAETLNRLS VYAR